1rsg

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{{STRUCTURE_1rsg| PDB=1rsg | SCENE= }}
{{STRUCTURE_1rsg| PDB=1rsg | SCENE= }}
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'''Crystal structure of the polyamine oxidase Fms1 from yeast'''
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===Crystal structure of the polyamine oxidase Fms1 from yeast===
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==Overview==
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Fms1 is a rate-limiting enzyme for the biosynthesis of pantothenic acid in yeast. Fms1 has polyamine oxidase (PAO) activity, which converts spermine into spermidine and 3-aminopropanal. The 3-aminopropanal is further oxidized to produce beta-alanine, which is necessary for the biosynthesis of pantothenic acid. The crystal structures of Fms1 and its complex with the substrate spermine have been determined using the single-wavelength anomalous diffraction (SAD) phasing method. Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain. The active site is a tunnel located at the interface of the two domains. The substrate spermine binds to the active site mainly via hydrogen bonds and hydrophobic interactions. In the complex, C11 but not C9 of spermine is close enough to the catalytic site (N5 of FAD) to be oxidized. Therefore, the products are spermidine and 3-aminopropanal, rather than 3-(aminopropyl) 4-aminobutyraldehyde and 1,3-diaminoprone.
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(as it appears on PubMed at http://www.pubmed.gov), where 15843025 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15843025}}
==About this Structure==
==About this Structure==
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[[Category: Liu, Q.]]
[[Category: Liu, Q.]]
[[Category: Fad binding motif]]
[[Category: Fad binding motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:51:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:45:42 2008''

Revision as of 05:45, 29 July 2008

Template:STRUCTURE 1rsg

Crystal structure of the polyamine oxidase Fms1 from yeast

Template:ABSTRACT PUBMED 15843025

About this Structure

1RSG is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structures of Fms1 and its complex with spermine reveal substrate specificity., Huang Q, Liu Q, Hao Q, J Mol Biol. 2005 May 13;348(4):951-9. PMID:15843025

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