3KB6

Crystal structure of D-Lactate dehydrogenase from aquifex aeolicus complexed with NAD and Lactic acid

Replaces:  2PI1

Summary for 3KB6

• Entry DOI: 10.2210/pdb3kb6/pdb
• Descriptor: D-lactate dehydrogenase, PROPANOIC ACID, LACTIC ACID, ... (8 entities in total)
• Functional Keywords: oxidoreductase, d-ldh, nad, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 4
• Total formula weight: 161199.18

Authors

Antonyuk, S.V.,Strange, R.W.,Ellis, M.J.,Bessho, Y.,Kuramitsu, S.,Yokoyama, S.,Hasnain, S.S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-10-20, release date: 2009-11-10, Last modification date: 2023-11-15)

Primary citation

Antonyuk, S.V.,Strange, R.W.,Ellis, M.J.,Bessho, Y.,Kuramitsu, S.,Inoue, Y.,Yokoyama, S.,Hasnain, S.S.
Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed with NAD(+) and lactic acid (or pyruvate).
Acta Crystallogr.,Sect.F, 65:1209-1213, 2009

PubMed Abstract: The crystal structure of D-lactate dehydrogenase from Aquifex aeolicus (aq_727) was determined to 2.12 A resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 90.94, b = 94.43, c = 188.85 A. The structure was solved by molecular replacement using the coenzyme-binding domain of Lactobacillus helveticus D-lactate dehydrogenase and contained two homodimers in the asymmetric unit. Each subunit of the homodimer was found to be in a ;closed' conformation with the NADH cofactor bound to the coenzyme-binding domain and with a lactate (or pyruvate) molecule bound at the interdomain active-site cleft.

PubMed: 20054113
DOI: 10.1107/S1744309109044935

Experimental method

X-RAY DIFFRACTION (2.12 Å)