1ie7: Difference between revisions

Revision as of 10:50, 1 July 2008

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File:1ie7.png

Template:STRUCTURE 1ie7

PHOSPHATE INHIBITED BACILLUS PASTEURII UREASE CRYSTAL STRUCTUREPHOSPHATE INHIBITED BACILLUS PASTEURII UREASE CRYSTAL STRUCTURE

Template:ABSTRACT PUBMED 11713685

About this StructureAbout this Structure

1IE7 is a Protein complex structure of sequences from Sporosarcina pasteurii. Full crystallographic information is available from OCA.

ReferenceReference

Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism., Benini S, Rypniewski WR, Wilson KS, Ciurli S, Mangani S, J Biol Inorg Chem. 2001 Oct;6(8):778-90. PMID:11713685

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-'''PHOSPHATE INHIBITED BACILLUS PASTEURII UREASE CRYSTAL STRUCTURE'''
+===PHOSPHATE INHIBITED BACILLUS PASTEURII UREASE CRYSTAL STRUCTURE===
-==Overview==
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-The structure of Bacillus pasteurii urease (BPU) inhibited with phosphate was solved and refined using synchrotron X-ray diffraction data from a vitrified crystal (1.85 A resolution, 99.3% completeness, data redundancy 4.6, R-factor 17.3%, PDB code 6UBP). A distance of 3.5 A separates the two Ni ions in the active site. The binding mode of the inhibitor involves the formation of four coordination bonds with the two Ni ions: one phosphate oxygen atom symmetrically bridges the two metal ions (1.9-2.0 A), while two of the remaining phosphate oxygen atoms bind to the Ni atoms at 2.4 A. The fourth phosphate oxygen is directed into the active site channel. Analysis of the H-bonding network around the bound inhibitor indicates that phosphate is bound as the H2PO4- anion, and that an additional proton is present on the Odelta2 atom of Asp(alpha363), an active site residue involved in Ni coordination through Odelta1. The flexible flap flanking the active site cavity is in the open conformation. Analysis of the complex reveals why phosphate is a relatively weak inhibitor and why sulfate does not bind to the nickels in the active site. The implications of the results for the understanding of the urease catalytic mechanism are reviewed. A novel alternative for the proton donor is presented.
+The line below this paragraph, {{ABSTRACT_PUBMED_11713685}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11713685 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11713685}}
 ==About this Structure==
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 [[Category: Nickel]]
 [[Category: Urease]]
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