2ohy: Difference between revisions

Revision as of 07:08, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ohy.png

Template:STRUCTURE 2ohy

X-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporusX-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporus

Template:ABSTRACT PUBMED 17516659

About this StructureAbout this Structure

2OHY is a Single protein structure of sequence from Streptomyces globisporus. Full crystallographic information is available from OCA.

ReferenceReference

The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway., Christianson CV, Montavon TJ, Van Lanen SG, Shen B, Bruner SD, Biochemistry. 2007 Jun 19;46(24):7205-14. Epub 2007 May 22. PMID:17516659

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OCA

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-'''X-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporus'''
+===X-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporus===
-==Overview==
+<!--
-The SgcC4 l-tyrosine 2,3-aminomutase (SgTAM) catalyzes the formation of (S)-beta-tyrosine in the biosynthetic pathway of the enediyne antitumor antibiotic C-1027. SgTAM is homologous to the histidine ammonia lyase family of enzymes whose activity is dependent on the methylideneimidazole-5-one (MIO) cofactor. Unlike the lyase enzymes, SgTAM catalyzes additional chemical transformations resulting in an overall stereospecific 1,2-amino shift in the substrate l-tyrosine to generate (S)-beta-tyrosine. Previously, we provided kinetic, spectroscopic, and mutagenesis data supporting the presence of MIO in the active site of SgTAM [Christenson, S. D.; Wu, W.; Spies, A.; Shen, B.; and Toney, M. D. (2003) Biochemistry 42, 12708-12718]. Here we report the first X-ray crystal structure of an MIO-containing aminomutase, SgTAM, and confirm the structural homology of SgTAM to ammonia lyases. Comparison of the structure of SgTAM to the l-tyrosine ammonia lyase from Rhodobacter sphaeroides provides insight into the structural basis for aminomutase activity. The results show that SgTAM has a closed active site well suited to retain ammonia and minimize the formation of lyase elimination products. The amino acid determinants for substrate recognition and catalysis can be predicted from the structure, setting the framework for detailed mechanistic investigations.
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+{{ABSTRACT_PUBMED_17516659}}
 ==About this Structure==
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 [[Category: 4-methylideneimidizole-5-one]]
 [[Category: Mio]]
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