1pzc: Difference between revisions
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pzc ConSurf]. | ||
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Revision as of 20:59, 9 February 2016
APO-PSEUDOAZURIN (METAL FREE PROTEIN)APO-PSEUDOAZURIN (METAL FREE PROTEIN)
Structural highlights
Function[AZUP_ALCFA] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 3D structure of the apo-pseudoazurin (copper free pseudoazurin) from Alcaligenes faecalis strain S-6 is determined and refined at pH 6.7 using X-ray diffraction data to 1.85 A resolution. The final crystallographic R-factor is 0.164. Comparing the structures of apo-pseudoazurin and the native (Cu2+) protein, we observed limited differences ranging between 0.1-0.4 A at the vicinity of the copper site, at the loops connecting the secondary structural elements, at certain beta-strands and at the amino and carboxy termini of the protein. The crystal structure of apo-pseudoazurin from Alcaligenes faecalis S-6.,Petratos K, Papadovasilaki M, Dauter Z FEBS Lett. 1995 Jul 24;368(3):432-4. PMID:7635192[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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