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1oat

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[[Category: pyridoxal phosphate]]
[[Category: pyridoxal phosphate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:54:24 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:48:26 2007''

Revision as of 13:43, 30 October 2007

Image:1oat.gif

1oat, resolution 2.5Å

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ORNITHINE AMINOTRANSFERASE

Overview

Ornithine aminotransferase (OAT), a pyridoxal-5'-phosphate dependent, enzyme, catalyses the transfer of the delta-amino group of L-ornithine to, 2-oxoglutarate, producing L-glutamate-gamma-semialdehyde, which, spontaneously cyclizes to pyrroline-5-carboxylate, and L-glutamate. The, crystal structure determination of human recombinant OAT is described in, this paper. As a first step, the structure was determined at low, resolution (6 A) by molecular replacement using the refined structure of, dialkylglycine decarboxylase as a search model. Crystallographic phases, were then refined and extended in a step-wise fashion to 2.5 A by cyclic, averaging of the electron density corresponding to the three monomers, within the asymmetric unit. Interpretation of the resulting map was, straightforward ... [(full description)]

About this Structure

1OAT is a [Single protein] structure of sequence from [Homo sapiens] with PLP as [ligand]. Active as [Ornithine aminotransferase], with EC number [2.6.1.13]. Structure known Active Sites: PLA, PLB and PLC. Full crystallographic information is available from [OCA].

Reference

Crystal structure of human recombinant ornithine aminotransferase., Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T, J Mol Biol. 1998 Mar 20;277(1):81-102. PMID:9514741

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