From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1dnu.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1dnu.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1dnu| PDB=1dnu | SCENE= }} | | {{STRUCTURE_1dnu| PDB=1dnu | SCENE= }} |
| | | | |
| - | '''STRUCTURAL ANALYSES OF HUMAN MYELOPEROXIDASE-THIOCYANATE COMPLEX'''
| + | ===STRUCTURAL ANALYSES OF HUMAN MYELOPEROXIDASE-THIOCYANATE COMPLEX=== |
| | | | |
| | | | |
| - | ==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. | + | 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. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11705390}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | [[Category: Peroxidase]] | | [[Category: Peroxidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:03:45 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:20:55 2008'' |
Revision as of 20:20, 30 June 2008
Template:STRUCTURE 1dnu
STRUCTURAL ANALYSES OF HUMAN MYELOPEROXIDASE-THIOCYANATE COMPLEX
Template:ABSTRACT PUBMED 11705390
About this Structure
1DNU is a Protein complex structure of sequences from Homo sapiens. 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 Mon Jun 30 23:20:55 2008
