2BKW

Yeast alanine:glyoxylate aminotransferase YFL030w

Summary for 2BKW

• Entry DOI: 10.2210/pdb2bkw/pdb
• Descriptor: ALANINE-GLYOXYLATE AMINOTRANSFERASE 1, PYRIDOXAL-5'-PHOSPHATE, GLYOXYLIC ACID, ... (4 entities in total)
• Functional Keywords: analine-glyoxylate aminotransferase, pyridoxal-5-phosphate, sad, glycolate pathway, transferase
• Biological source: SACCHAROMYCES CEREVISIAE S288C (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 42604.49

Authors

Meyer, P.,Liger, D.,Leulliot, N.,Quevillon-Cheruel, S.,Zhou, C.Z.,Borel, F.,Ferrer, J.L.,Poupon, A.,Janin, J.,van Tilbeurgh, H. (deposition date: 2005-02-21, release date: 2005-11-02, Last modification date: 2025-04-09)

Primary citation

Meyer, P.,Liger, D.,Leulliot, N.,Quevillon-Cheruel, S.,Zhou, C.Z.,Borel, F.,Ferrer, J.L.,Poupon, A.,Janin, J.,Van Tilbeurgh, H.
Crystal Structure and Confirmation of the Alanine:Glyoxylate Aminotransferase Activity of the Yfl030W Yeast Protein
Biochimie, 87:1041-, 2005

PubMed Abstract: We have determined the three-dimensional crystal structure of the protein encoded by the open reading frame YFL030w from Saccharomyces cerevisiae to a resolution of 2.6 A using single wavelength anomalous diffraction. YFL030w is a 385 amino-acid protein with sequence similarity to the aminotransferase family. The structure of the protein reveals a homodimer adopting the fold-type I of pyridoxal 5'-phosphate (PLP)-dependent aminotransferases. The PLP co-factor is covalently bound to the active site in the crystal structure. The protein shows close structural resemblance with the human alanine:glyoxylate aminotransferase (EC 2.6.1.44), an enzyme involved in the hereditary kidney stone disease primary hyperoxaluria type 1. In this paper we show that YFL030w codes for an alanine:glyoxylate aminotransferase, highly specific for its amino donor and acceptor substrates.

PubMed: 16226833
DOI: 10.1016/J.BIOCHI.2005.09.001

Experimental method

X-RAY DIFFRACTION (2.57 Å)