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1aop

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{{STRUCTURE_1aop| PDB=1aop | SCENE= }}
{{STRUCTURE_1aop| PDB=1aop | SCENE= }}
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'''SULFITE REDUCTASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION'''
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===SULFITE REDUCTASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION===
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==Overview==
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Fundamental chemical transformations for biogeochemical cycling of sulfur and nitrogen are catalyzed by sulfite and nitrite reductases. The crystallographic structure of Escherichia coli sulfite reductase hemoprotein (SiRHP), which catalyzes the concerted six-electron reductions of sulfite to sulfide and nitrite to ammonia, was solved with multiwavelength anomalous diffraction (MAD) of the native siroheme and Fe4S4 cluster cofactors, multiple isomorphous replacement, and selenomethionine sequence markers. Twofold symmetry within the 64-kilodalton polypeptide generates a distinctive three-domain alpha/beta fold that controls cofactor assembly and reactivity. Homology regions conserved between the symmetry-related halves of SiRHP and among other sulfite and nitrite reductases revealed key residues for stability and function, and identified a sulfite or nitrite reductase repeat (SNiRR) common to a redox-enzyme superfamily. The saddle-shaped siroheme shares a cysteine thiolate ligand with the Fe4S4 cluster and ligates an unexpected phosphate anion. In the substrate complex, sulfite displaces phosphate and binds to siroheme iron through sulfur. An extensive hydrogen-bonding network of positive side chains, water molecules, and siroheme carboxylates activates S-O bonds for reductive cleavage.
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(as it appears on PubMed at http://www.pubmed.gov), where 7569952 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7569952}}
==About this Structure==
==About this Structure==
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[[Category: Six-electron reduction]]
[[Category: Six-electron reduction]]
[[Category: Snirr]]
[[Category: Snirr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:31:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:18:28 2008''

Revision as of 14:18, 30 June 2008

Image:1aop.png

Template:STRUCTURE 1aop

SULFITE REDUCTASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 7569952

About this Structure

1AOP is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1geo. Full crystallographic information is available from OCA.

Reference

Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions., Crane BR, Siegel LM, Getzoff ED, Science. 1995 Oct 6;270(5233):59-67. PMID:7569952

Page seeded by OCA on Mon Jun 30 17:18:28 2008

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