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1a8c

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(New page: 200px<br /><applet load="1a8c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a8c" /> '''PRIMARY SEQUENCE AND SOLUTION CONFORMATION O...)
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[[Image:1a8c.gif|left|200px]]<br /><applet load="1a8c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a8c" />
 
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'''PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERROCYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITHOUT HYDROGEN BOND CONSTRAINTS'''<br />
 
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==Overview==
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==PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERROCYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITHOUT HYDROGEN BOND CONSTRAINTS==
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Cytochrome c-552 from Nitrosomonas europaea is a 9.1-kDa monoheme protein, that is a member of the bacterial cytochrome c-551 family. The gene, encoding for c-552 has been cloned and sequenced and the primary sequence, of the product deduced. Proton resonance assignments were made for all, main-chain and most side-chain protons in the diamagnetic, reduced form by, two-dimensional NMR techniques. Distance constraints (1056) were, determined from nuclear Overhauser enhancements, and torsion angle, constraints (88) were determined from scalar coupling estimates. Solution, conformations for the protein were computed by the hybrid distance, geometry-simulated annealing approach. For 20 computed structures, the, root mean squared deviation from the average position of equivalent atoms, was 0.84 A (sigma = 0.12) for backbone atoms over all residues. Analysis, by residue revealed there were three regions clearly less well defined, than the rest of the protein: the first two residues at the N-terminus, the last two at the C-terminus, and a loop region from residues 34 to 40., Omitting these regions from the comparison, the root mean squared, deviation was 0.61 A (sigma = 0.13) for backbone atoms, 0.86 A (sigma =, 0.12) for all associated heavy atoms, and 0. 43 A (sigma = 0.17) for the, heme group. The global folding of the protein is consistent with others in, the c-551 family. A deletion at the N-terminus relative to other family, members had no impact on the global folding, whereas an insertion at, residue 65 did affect the way the polypeptide packs against the, methionine-ligated side of the heme. The effects of specific substitutions, will be discussed. The structure of c-552 serves to delineate essential, features of the c-551 family.
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<StructureSection load='1a8c' size='340' side='right'caption='[[1a8c]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1a8c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8C FirstGlance]. <br>
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1A8C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A8C OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8c OCA], [https://pdbe.org/1a8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8c RCSB], [https://www.ebi.ac.uk/pdbsum/1a8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8c ProSAT]</span></td></tr>
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Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea., Timkovich R, Bergmann D, Arciero DM, Hooper AB, Biophys J. 1998 Oct;75(4):1964-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9746537 9746537]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CY552_NITEU CY552_NITEU] Monoheme c-type cytochrome. Probable electron donor to membrane cytochrome oxidase and to periplasmic nitrite reductase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/main_output.php?pdb_ID=1a8c ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Nitrosomonas europaea]]
[[Category: Nitrosomonas europaea]]
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[[Category: Single protein]]
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[[Category: Arciero DM]]
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[[Category: Arciero, D.M.]]
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[[Category: Bergmann D]]
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[[Category: Bergmann, D.]]
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[[Category: Hooper AB]]
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[[Category: Hooper, A.B.]]
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[[Category: Timkovich R]]
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[[Category: Timkovich, R.]]
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[[Category: HEC]]
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[[Category: cytochrome]]
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[[Category: hemoprotein]]
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[[Category: prokaryotic electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:40:39 2007''
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Current revision

PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERROCYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITHOUT HYDROGEN BOND CONSTRAINTS

PDB ID 1a8c

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