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Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.

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Title: Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
Authors: Anand, Kanchan, Mathur, Divya, Anant, Avishek, Garg, Lalit C.
Source: Acta Crystallographica: Section F (Wiley-Blackwell). May2010, Vol. 66 Issue 5, p490-497. 8p.
Subjects: Glucose phosphate isomerase, Mycobacterium tuberculosis, Crystal structure, Bacterial enzymes, Autocrine mechanisms
Abstract: Phosphoglucose isomerase (PGI) plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. PGI is also known to act as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator. Here, the first crystal structure of PGI from Mycobacterium tuberculosis H37Rv (Mtb) is reported. The structure was refined at 2.25 Å resolution and revealed the presence of one molecule in the asymmetric unit with two globular domains. As known previously, the active site of Mtb PGI contains conserved residues including Glu356, Glu216 and His387 (where His387 is from the neighbouring molecule). The crystal structure of Mtb PGI was observed to be rather more similar to human PGI than other nonbacterial PGIs, with only a few differences being detected in the loops, arm and hook regions of the human and Mtb PGIs, suggesting that the M. tuberculosis enzyme uses the same enzyme mechanism. [ABSTRACT FROM AUTHOR]
Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell 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: Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
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  Data: <searchLink fieldCode="AR" term="%22Anand%2C+Kanchan%22">Anand, Kanchan</searchLink><br /><searchLink fieldCode="AR" term="%22Mathur%2C+Divya%22">Mathur, Divya</searchLink><br /><searchLink fieldCode="AR" term="%22Anant%2C+Avishek%22">Anant, Avishek</searchLink><br /><searchLink fieldCode="AR" term="%22Garg%2C+Lalit+C%2E%22">Garg, Lalit C.</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Acta+Crystallographica%3A+Section+F+%28Wiley-Blackwell%29%22">Acta Crystallographica: Section F (Wiley-Blackwell)</searchLink>. May2010, Vol. 66 Issue 5, p490-497. 8p.
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  Data: <searchLink fieldCode="DE" term="%22Glucose+phosphate+isomerase%22">Glucose phosphate isomerase</searchLink><br /><searchLink fieldCode="DE" term="%22Mycobacterium+tuberculosis%22">Mycobacterium tuberculosis</searchLink><br /><searchLink fieldCode="DE" term="%22Crystal+structure%22">Crystal structure</searchLink><br /><searchLink fieldCode="DE" term="%22Bacterial+enzymes%22">Bacterial enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Autocrine+mechanisms%22">Autocrine mechanisms</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: Phosphoglucose isomerase (PGI) plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. PGI is also known to act as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator. Here, the first crystal structure of PGI from Mycobacterium tuberculosis H37Rv (Mtb) is reported. The structure was refined at 2.25 Å resolution and revealed the presence of one molecule in the asymmetric unit with two globular domains. As known previously, the active site of Mtb PGI contains conserved residues including Glu356, Glu216 and His387 (where His387 is from the neighbouring molecule). The crystal structure of Mtb PGI was observed to be rather more similar to human PGI than other nonbacterial PGIs, with only a few differences being detected in the loops, arm and hook regions of the human and Mtb PGIs, suggesting that the M. tuberculosis enzyme uses the same enzyme mechanism. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell 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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        Value: 10.1107/S1744309110011656
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        Text: English
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        PageCount: 8
        StartPage: 490
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      – SubjectFull: Glucose phosphate isomerase
        Type: general
      – SubjectFull: Mycobacterium tuberculosis
        Type: general
      – SubjectFull: Crystal structure
        Type: general
      – SubjectFull: Bacterial enzymes
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      – SubjectFull: Autocrine mechanisms
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              Text: May2010
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              Y: 2010
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