1dnw: Difference between revisions

Revision as of 23:21, 30 June 2008

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File:1dnw.png

Template:STRUCTURE 1dnw

HUMAN MYELOPEROXIDASE-CYANIDE-THIOCYANATE COMPLEXHUMAN MYELOPEROXIDASE-CYANIDE-THIOCYANATE COMPLEX

Template:ABSTRACT PUBMED 11705390

About this StructureAbout this Structure

1DNW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution., Blair-Johnson M, Fiedler T, Fenna R, Biochemistry. 2001 Nov 20;40(46):13990-7. PMID:11705390

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-'''HUMAN MYELOPEROXIDASE-CYANIDE-THIOCYANATE COMPLEX'''
+===HUMAN MYELOPEROXIDASE-CYANIDE-THIOCYANATE COMPLEX===
-==Overview==
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-The 1.9 A X-ray crystal structure of human myeloperoxidase complexed with cyanide (R = 0.175, R(free) = 0.215) indicates that cyanide binds to the heme iron with a bent Fe-C-N angle of approximately 157 degrees, and binding is accompanied by movement of the iron atom by 0.2 A into the porphyrin plane. The bent orientation of the cyanide allows the formation of three hydrogen bonds between its nitrogen atom and the distal histidine as well as two water molecules in the distal cavity. The 1.85 A X-ray crystal structure of an inhibitory complex with thiocyanate (R = 0.178, R(free) = 0.210) indicates replacement of chloride at a proximal helix halide binding site in addition to binding in the distal cavity in an orientation parallel with the heme. The thiocyanate replaces two water molecules in the distal cavity and is hydrogen bonded to Gln 91. The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. These results support a model for a single common binding site for halides and thiocyanate as substrates or as inhibitors near the delta-meso carbon of the porphyrin ring in myeloperoxidase.
+The line below this paragraph, {{ABSTRACT_PUBMED_11705390}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11705390 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11705390}}
 ==About this Structure==
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 [[Category: Substrate complex]]
 [[Category: Thiocyanate]]
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