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Solution Nuclear Magnetic Resonance Structure of the GATase Subunit and Structural Basis of the Interaction between GATase and ATPPase Subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.

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Title: Solution Nuclear Magnetic Resonance Structure of the GATase Subunit and Structural Basis of the Interaction between GATase and ATPPase Subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Authors: Ali, Rustam1, Kumar, Sanjeev2, Balaram, Hemalatha2, Sarma, Siddhartha P.1 sidd@mbu.iisc.ernet.in
Source: Biochemistry. 6/25/2013, Vol. 52 Issue 25, p4308-4323. 6p.
Subjects: Methanocaldococcus jannaschii, Nuclear magnetic resonance, Glutamine amidotransferase, Guanosine monophosphate synthetase, Gel permeation chromatography, Pyrococcus horikoshii
Abstract: The solution structure of the monomeric glutamine amidotransferase (GATase) subunit of the Methanocaldococcus janaschii (Mj) guanosine monophosphate synthetase (GMPS) has been determined using high-resolution nuclear magnetic resonance methods. Gel filtration chromatography and 15N backbone relaxation studies have shown that the Mj GATase subunit is present in solution as a 21 kDa (188-residue) monomer. The ensemble of 20 lowest-energy structures showed root-mean-square deviations of 0.35 ± 0.06 Å for backbone atoms and 0.8 ± 0.06 Å for all heavy atoms. Furthermore, 99.4% of the backbone dihedral angles are present in the allowed region of the Ramachandran map, indicating the stereochemical quality of the structure. The core of the tertiary structure of the GATase is composed of a seven-stranded mixed β-sheet that is fenced by five α-helices. The Mj GATase is similar in structure to the Pyrococcus horikoshi (Ph) GATase subunit. Nuclear magnetic resonance (NMR) chemical shift perturbations and changes in line width were monitored to identify residues on GATase that were responsible for interaction with magnesium and the ATPPase subunit, respectively. These interaction studies showed that a common surface exists for the metal ion binding as well as for the protein-protein interaction. The dissociation constant for the GATase-Mg2+ interaction has been found to be 1 mM, which implies that interaction is very weak and falls in the fast chemical exchange regime. The GATase-ATPPase interaction, on the other hand, falls in the intermediate chemical exchange regime on the NMR time scale. The implication of this interaction in terms of the regulation of the GATase activity of holo GMPS is discussed. [ABSTRACT FROM AUTHOR]
Copyright of Biochemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Solution Nuclear Magnetic Resonance Structure of the GATase Subunit and Structural Basis of the Interaction between GATase and ATPPase Subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
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  Data: <searchLink fieldCode="AR" term="%22Ali%2C+Rustam%22">Ali, Rustam</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kumar%2C+Sanjeev%22">Kumar, Sanjeev</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Balaram%2C+Hemalatha%22">Balaram, Hemalatha</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Sarma%2C+Siddhartha+P%2E%22">Sarma, Siddhartha P.</searchLink><relatesTo>1</relatesTo><i> sidd@mbu.iisc.ernet.in</i>
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  Data: <searchLink fieldCode="JN" term="%22Biochemistry%22">Biochemistry</searchLink>. 6/25/2013, Vol. 52 Issue 25, p4308-4323. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Methanocaldococcus+jannaschii%22">Methanocaldococcus jannaschii</searchLink><br /><searchLink fieldCode="DE" term="%22Nuclear+magnetic+resonance%22">Nuclear magnetic resonance</searchLink><br /><searchLink fieldCode="DE" term="%22Glutamine+amidotransferase%22">Glutamine amidotransferase</searchLink><br /><searchLink fieldCode="DE" term="%22Guanosine+monophosphate+synthetase%22">Guanosine monophosphate synthetase</searchLink><br /><searchLink fieldCode="DE" term="%22Gel+permeation+chromatography%22">Gel permeation chromatography</searchLink><br /><searchLink fieldCode="DE" term="%22Pyrococcus+horikoshii%22">Pyrococcus horikoshii</searchLink>
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  Label: Abstract
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  Data: The solution structure of the monomeric glutamine amidotransferase (GATase) subunit of the Methanocaldococcus janaschii (Mj) guanosine monophosphate synthetase (GMPS) has been determined using high-resolution nuclear magnetic resonance methods. Gel filtration chromatography and 15N backbone relaxation studies have shown that the Mj GATase subunit is present in solution as a 21 kDa (188-residue) monomer. The ensemble of 20 lowest-energy structures showed root-mean-square deviations of 0.35 ± 0.06 Å for backbone atoms and 0.8 ± 0.06 Å for all heavy atoms. Furthermore, 99.4% of the backbone dihedral angles are present in the allowed region of the Ramachandran map, indicating the stereochemical quality of the structure. The core of the tertiary structure of the GATase is composed of a seven-stranded mixed β-sheet that is fenced by five α-helices. The Mj GATase is similar in structure to the Pyrococcus horikoshi (Ph) GATase subunit. Nuclear magnetic resonance (NMR) chemical shift perturbations and changes in line width were monitored to identify residues on GATase that were responsible for interaction with magnesium and the ATPPase subunit, respectively. These interaction studies showed that a common surface exists for the metal ion binding as well as for the protein-protein interaction. The dissociation constant for the GATase-Mg2+ interaction has been found to be 1 mM, which implies that interaction is very weak and falls in the fast chemical exchange regime. The GATase-ATPPase interaction, on the other hand, falls in the intermediate chemical exchange regime on the NMR time scale. The implication of this interaction in terms of the regulation of the GATase activity of holo GMPS is discussed. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Biochemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1021/bi400472e
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      – Code: eng
        Text: English
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        PageCount: 6
        StartPage: 4308
    Subjects:
      – SubjectFull: Methanocaldococcus jannaschii
        Type: general
      – SubjectFull: Nuclear magnetic resonance
        Type: general
      – SubjectFull: Glutamine amidotransferase
        Type: general
      – SubjectFull: Guanosine monophosphate synthetase
        Type: general
      – SubjectFull: Gel permeation chromatography
        Type: general
      – SubjectFull: Pyrococcus horikoshii
        Type: general
    Titles:
      – TitleFull: Solution Nuclear Magnetic Resonance Structure of the GATase Subunit and Structural Basis of the Interaction between GATase and ATPPase Subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
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            NameFull: Ali, Rustam
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            NameFull: Kumar, Sanjeev
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            NameFull: Balaram, Hemalatha
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            NameFull: Sarma, Siddhartha P.
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            – D: 25
              M: 06
              Text: 6/25/2013
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              Y: 2013
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              Value: 52
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            – TitleFull: Biochemistry
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