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1ygy

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{{STRUCTURE_1ygy| PDB=1ygy | SCENE= }}
{{STRUCTURE_1ygy| PDB=1ygy | SCENE= }}
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'''Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis'''
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===Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis===
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==Overview==
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Phosphoglycerate dehydrogenases exist in at least three different structural motifs. The first D-3-phosphoglycerate dehydrogenase structure to be determined was from Escherichia coli and is a tetramer composed of identical subunits that contain three discernable structural domains. The crystal structure of D-3-phosphoglycerate dehydrogenase from Mycobacterium tuberculosis has been determined at 2.3 A. This enzyme represents a second structural motif of the D-3-phosphoglycerate dehydrogenase family, one that contains an extended C-terminal region. This structure is also a tetramer of identical subunits, and the extended motif of 135 amino acids exists as a fourth structural domain. This intervening domain exerts quite a surprising characteristic to the structure by introducing significant asymmetry in the tetramer. The asymmetric unit is composed of two identical subunits that exist in two different conformations characterized by rotation of approximately 180 degrees around a hinge connecting two of the four domains. This asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. As a result, the surface of the intervening domain that is exposed to solvent in one subunit is turned inward in the other subunit toward the center of the structure where it makes contact with other structural elements. Significant asymmetry is also seen at the subunit level where different conformations exist at the NAD-binding site and the putative serine-binding site in the two unique subunits.
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{{ABSTRACT_PUBMED_15668249}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits., Dey S, Grant GA, Sacchettini JC, J Biol Chem. 2005 Apr 15;280(15):14892-9. Epub 2005 Jan 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15668249 15668249]
Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits., Dey S, Grant GA, Sacchettini JC, J Biol Chem. 2005 Apr 15;280(15):14892-9. Epub 2005 Jan 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15668249 15668249]
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D-3-Phosphoglycerate dehydrogenase from Mycobacterium tuberculosis is a link between the Escherichia coli and mammalian enzymes., Dey S, Hu Z, Xu XL, Sacchettini JC, Grant GA, J Biol Chem. 2005 Apr 15;280(15):14884-91. Epub 2005 Jan 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15668250 15668250]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Phosphoglycerate dehydrogenase]]
[[Category: Phosphoglycerate dehydrogenase]]
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[[Category: Tb structural genomics consortium]]
[[Category: Tb structural genomics consortium]]
[[Category: Tbsgc]]
[[Category: Tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:18:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:02:44 2008''

Revision as of 16:02, 27 July 2008

Image:1ygy.png

Template:STRUCTURE 1ygy

Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis

Template:ABSTRACT PUBMED 15668249

About this Structure

1YGY is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits., Dey S, Grant GA, Sacchettini JC, J Biol Chem. 2005 Apr 15;280(15):14892-9. Epub 2005 Jan 24. PMID:15668249

D-3-Phosphoglycerate dehydrogenase from Mycobacterium tuberculosis is a link between the Escherichia coli and mammalian enzymes., Dey S, Hu Z, Xu XL, Sacchettini JC, Grant GA, J Biol Chem. 2005 Apr 15;280(15):14884-91. Epub 2005 Jan 24. PMID:15668250

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