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New page: left|200px<br /><applet load="1cor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cor" /> '''INVESTIGATION OF THE SOLUTION CONFORMATION O... |
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== | ==INVESTIGATION OF THE SOLUTION CONFORMATION OF CYTOCHROME C-551 FROM PSEUDOMONAS STUTZERI== | ||
1H NMR spectroscopy and solution structure computations have been used to | <StructureSection load='1cor' size='340' side='right'caption='[[1cor]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1cor]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cor OCA], [https://pdbe.org/1cor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cor RCSB], [https://www.ebi.ac.uk/pdbsum/1cor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cor ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CY551_STUST CY551_STUST] Electron donor for cytochrome cd1 in nitrite and nitrate respiration. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1cor_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1cor ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
1H NMR spectroscopy and solution structure computations have been used to examine ferrocytochrome c-551 from Pseudomonas stutzeri (ATCC 17588). Resonance assignments are proposed for all main-chain and most side-chain protons. Distance constraints were determined on the basis of nuclear Overhauser enhancements between pairs of protons. Dihedral angle constraints were determined from estimates of scaler coupling constants. Twenty-four structures were calculated by distance geometry and refined by energy minimization and simulated annealing on the basis of 1033 interproton distance and 57 torsion angle constraints. Both the main-chain and side-chain atoms are well defined except for a loop region around residues 34-40, the first two residues at the N-terminus and the last two at the C-terminus, and some side chains located on the molecular surface. The average root mean squared deviation in position for equivalent atoms between the 24 individual structures and the mean structure obtained by averaging their coordinates is 0.54 +/- 0.08 A for the main-chain atoms and 0.97 +/- 0.09 A for all non-hydrogen atoms of residues 3-80 plus the heme group. These structures were compared to the X-ray crystallographic structure of an analogous protein, cytochrome c-551 from Pseudomonas aeruginosa [Matsuura, Takano, & Dickerson (1982) J. Mol. Biol. 156, 389-409). The main-chain folding patterns are very consistent, but there are some differences. The largest difference is in a surface loop segment from residues 34 to 40. | |||
Investigation of the solution conformation of cytochrome c-551 from Pseudomonas stutzeri.,Cai M, Bradford EG, Timkovich R Biochemistry. 1992 Sep 15;31(36):8603-12. PMID:1327105<ref>PMID:1327105</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cor" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas stutzeri]] | [[Category: Pseudomonas stutzeri]] | ||
[[Category: Bradford EG]] | |||
[[Category: Bradford | [[Category: Cai M]] | ||
[[Category: Cai | [[Category: Timkovich R]] | ||
[[Category: Timkovich | |||
Latest revision as of 09:29, 30 October 2024
INVESTIGATION OF THE SOLUTION CONFORMATION OF CYTOCHROME C-551 FROM PSEUDOMONAS STUTZERIINVESTIGATION OF THE SOLUTION CONFORMATION OF CYTOCHROME C-551 FROM PSEUDOMONAS STUTZERI
Structural highlights
FunctionCY551_STUST Electron donor for cytochrome cd1 in nitrite and nitrate respiration. 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 PubMed1H NMR spectroscopy and solution structure computations have been used to examine ferrocytochrome c-551 from Pseudomonas stutzeri (ATCC 17588). Resonance assignments are proposed for all main-chain and most side-chain protons. Distance constraints were determined on the basis of nuclear Overhauser enhancements between pairs of protons. Dihedral angle constraints were determined from estimates of scaler coupling constants. Twenty-four structures were calculated by distance geometry and refined by energy minimization and simulated annealing on the basis of 1033 interproton distance and 57 torsion angle constraints. Both the main-chain and side-chain atoms are well defined except for a loop region around residues 34-40, the first two residues at the N-terminus and the last two at the C-terminus, and some side chains located on the molecular surface. The average root mean squared deviation in position for equivalent atoms between the 24 individual structures and the mean structure obtained by averaging their coordinates is 0.54 +/- 0.08 A for the main-chain atoms and 0.97 +/- 0.09 A for all non-hydrogen atoms of residues 3-80 plus the heme group. These structures were compared to the X-ray crystallographic structure of an analogous protein, cytochrome c-551 from Pseudomonas aeruginosa [Matsuura, Takano, & Dickerson (1982) J. Mol. Biol. 156, 389-409). The main-chain folding patterns are very consistent, but there are some differences. The largest difference is in a surface loop segment from residues 34 to 40. Investigation of the solution conformation of cytochrome c-551 from Pseudomonas stutzeri.,Cai M, Bradford EG, Timkovich R Biochemistry. 1992 Sep 15;31(36):8603-12. PMID:1327105[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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