2YEP

STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE

Replaces:  2W4N

Summary for 2YEP

• Entry DOI: 10.2210/pdb2yep/pdb
• Related: 1VZ6 1VZ7 1VZ8 2V4I 2VZK 2W4N
• Descriptor: GLUTAMATE N-ACETYLTRANSFERASE 2 ALPHA CHAIN, GLUTAMATE N-ACETYLTRANSFERASE 2 BETA CHAIN, GLUTAMIC ACID, ... (6 entities in total)
• Functional Keywords: acyl enzyme, transferase, ntn hydrolase, acyltransferase, ornithine acetyl transferase, hydrolase
• Biological source: STREPTOMYCES CLAVULIGERUS; More
• Total number of polymer chains: 8
• Total formula weight: 167225.22

Authors

Chowdhury, R.,Iqbal, A.,Clifton, I.J.,Schofield, C.J. (deposition date: 2011-03-29, release date: 2011-09-07, Last modification date: 2024-11-13)

Primary citation

Iqbal, A.,Clifton, I.J.,Chowdhury, R.,Ivison, D.,Domene, C.,Schofield, C.J.
Structural and Biochemical Analyses Reveal How Ornithine Acetyl Transferase Binds Acidic and Basic Amino Acid Substrates.
Org.Biomol.Chem., 9:6219-, 2011

PubMed Abstract: Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes.

PubMed: 21796301
DOI: 10.1039/C1OB05554B

Experimental method

X-RAY DIFFRACTION (2.7 Å)