1d5l
From Proteopedia
(New page: 200px<br /> <applet load="1d5l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5l, resolution 1.90Å" /> '''CRYSTAL STRUCTURE O...) |
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caption="1d5l, resolution 1.90Å" /> | caption="1d5l, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF CYANIDE-BOUND HUMAN MYELOPEROXIDASE ISOFORM C AT PH 5.5'''<br /> | '''CRYSTAL STRUCTURE OF CYANIDE-BOUND HUMAN MYELOPEROXIDASE ISOFORM C AT PH 5.5'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1D5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, CA, CL, SO4, ACT, CYN and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http:// | + | 1D5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CYN:'>CYN</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxidase-cyanide complex]] | [[Category: peroxidase-cyanide complex]] | ||
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Revision as of 13:38, 15 February 2008
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CRYSTAL STRUCTURE OF CYANIDE-BOUND HUMAN MYELOPEROXIDASE ISOFORM C AT PH 5.5
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Alzheimer disease, susceptibility to OMIM:[606989], Lung cancer, protection against, in smokers OMIM:[606989], Myeloperoxidase deficiency OMIM:[606989]
About this Structure
1D5L is a Single protein structure of sequence from Homo sapiens with , , , , , and as ligands. Active as Peroxidase, with EC number 1.11.1.7 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Fri Feb 15 15:38:36 2008
Categories: Homo sapiens | Peroxidase | Single protein | Davey, C.A. | Fenna, R.E. | Fiedler, T.J. | ACT | CA | CL | CYN | HEM | NAG | SO4 | Heme-protein | Oxidoreductase | Peroxidase-cyanide complex
