1zps: Difference between revisions

Revision as of 09:49, 29 July 2008

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File:1zps.png

Template:STRUCTURE 1zps

Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisICrystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI

Template:ABSTRACT PUBMED 16042384

About this StructureAbout this Structure

1ZPS is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI., Sivaraman J, Myers RS, Boju L, Sulea T, Cygler M, Jo Davisson V, Schrag JD, Biochemistry. 2005 Aug 2;44(30):10071-80. PMID:16042384

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OCA

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-[[Image:1zps.gif|left|200px]]
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-'''Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI'''
+===Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI===
-==Overview==
+<!--
-The metabolic pathway for histidine biosynthesis is interesting from an evolutionary perspective because of the diversity of gene organizations and protein structures involved. Hydrolysis of phosphoribosyl-AMP, the third step in the histidine biosynthetic pathway, is carried out by PR-AMP cyclohydrolase, the product of the hisI gene. The three-dimensional structure of PR-AMP cyclohydrolase from Methanobacterium thermoautotrophicum was solved and refined to 1.7 A resolution. The enzyme is a homodimer. The position of the Zn(2+)-binding site that is essential for catalysis was inferred from the positions of bound Cd(2+) ions, which were part of the crystallization medium. These metal binding sites include three cysteine ligands, two from one monomer and the third from the second monomer. The enzyme remains active when Cd(2+) is substituted for Zn(2+). The likely binding site for Mg(2+), also necessary for activity in a homologous cyclohydrolase, was also inferred from Cd(2+) positions and is comprised of aspartic acid side chains. The putative substrate-binding cleft is formed at the interface between the two monomers of the dimer. This fact, combined with the localization of the Zn(2+)-binding site, indicates that the enzyme is an obligate dimer.
+The line below this paragraph, {{ABSTRACT_PUBMED_16042384}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16042384 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16042384}}
 ==About this Structure==
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 [[Category: Montreal-kingston bacterial structural genomics initiative]]
 [[Category: Structural genomic]]
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