1YGY

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

1YGY の概要

• エントリーDOI: 10.2210/pdb1ygy/pdb
• 分子名称: D-3-phosphoglycerate dehydrogenase, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: oxidoreductase, phosphoglycerate dehydrogenase, serine biosynthesis, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109860.38

構造登録者

Dey, S.,Grant, G.A.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (登録日: 2005-01-05, 公開日: 2005-01-25, 最終更新日: 2024-10-23)

主引用文献

Dey, S.,Grant, G.A.,Sacchettini, J.C.
Crystal Structure of Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase: EXTREME ASYMMETRY IN A TETRAMER OF IDENTICAL SUBUNITS
J.Biol.Chem., 280:14892-14899, 2005

PubMed Abstract: 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.

PubMed: 15668249
DOI: 10.1074/jbc.M414489200

実験手法

X-RAY DIFFRACTION (2.3 Å)