1ygy
From Proteopedia
(New page: 200px<br /><applet load="1ygy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ygy, resolution 2.30Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ygy.gif|left|200px]]<br /><applet load="1ygy" size=" | + | [[Image:1ygy.gif|left|200px]]<br /><applet load="1ygy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ygy, resolution 2.30Å" /> | caption="1ygy, resolution 2.30Å" /> | ||
'''Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis'''<br /> | '''Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphoglycerate dehydrogenases exist in at least three different | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YGY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with TAR as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_dehydrogenase Phosphoglycerate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.95 1.1.1.95] Full crystallographic information is available from [http:// | + | 1YGY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=TAR:'>TAR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_dehydrogenase Phosphoglycerate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.95 1.1.1.95] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dey, S.]] | [[Category: Dey, S.]] | ||
| - | [[Category: Grant, G | + | [[Category: Grant, G A.]] |
| - | [[Category: Sacchettini, J | + | [[Category: Sacchettini, J C.]] |
| - | [[Category: TBSGC, TB | + | [[Category: TBSGC, TB Structural Genomics Consortium.]] |
[[Category: TAR]] | [[Category: TAR]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
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[[Category: tbsgc]] | [[Category: tbsgc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:11 2008'' |
Revision as of 14:05, 21 February 2008
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Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis
Overview
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.
About this Structure
1YGY is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as Phosphoglycerate dehydrogenase, with EC number 1.1.1.95 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
Page seeded by OCA on Thu Feb 21 16:05:11 2008
Categories: Mycobacterium tuberculosis | Phosphoglycerate dehydrogenase | Single protein | Dey, S. | Grant, G A. | Sacchettini, J C. | TBSGC, TB Structural Genomics Consortium. | TAR | Oxidoreductase | Protein structure initiative | Psi | Serine biosynthesis | Structural genomics | Tb structural genomics consortium | Tbsgc
