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| | {{STRUCTURE_2h0f| PDB=2h0f | SCENE= }} | | {{STRUCTURE_2h0f| PDB=2h0f | SCENE= }} |
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| - | '''Crystal Structure of PucM in the presence of 8-azaxanthine'''
| + | ===Crystal Structure of PucM in the presence of 8-azaxanthine=== |
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| - | ==Overview==
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| - | The ureide pathway, which produces ureides from uric acid, is an essential purine catabolic process for storing and transporting the nitrogen fixed in leguminous plants and some bacteria. PucM from Bacillus subtilis was recently characterized and found to catalyze the second reaction of the pathway, hydrolyzing 5-hydroxyisourate (HIU), a product of uricase in the first step. PucM has 121 amino acid residues and shows high sequence similarity to the functionally unrelated protein transthyretin (TTR), a thyroid hormone-binding protein. Therefore, PucM belongs to the TTR-related proteins (TRP) family. The crystal structures of PucM at 2.0 A and its complexes with the substrate analogs 8-azaxanthine and 5,6-diaminouracil reveal that even with their overall structure similarity, homotetrameric PucM and TTR are completely different, both in their electrostatic potential and in the size of the active sites located at the dimeric interface. Nevertheless, the absolutely conserved residues across the TRP family, including His-14, Arg-49, His-105, and the C-terminal Tyr-118-Arg-119-Gly-120-Ser-121, indeed form the active site of PucM. Based on the results of site-directed mutagenesis of these residues, we propose a possible mechanism for HIU hydrolysis. The PucM structure determined for the TRP family leads to the conclusion that diverse members of the TRP family would function similarly to PucM as HIU hydrolase. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16782815}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16782815 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16782815}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Inhibitor complex]] | | [[Category: Inhibitor complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:43:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:01:32 2008'' |
Revision as of 21:01, 27 July 2008
Template:STRUCTURE 2h0f
Crystal Structure of PucM in the presence of 8-azaxanthine
Template:ABSTRACT PUBMED 16782815
About this Structure
2H0F is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family., Jung DK, Lee Y, Park SG, Park BC, Kim GH, Rhee S, Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9790-5. Epub 2006 Jun 16. PMID:16782815
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