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1a56

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[[Image:1a56.gif|left|200px]]
 
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{{Structure
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==PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERRICYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITH EXPLICIT HYDROGEN BOND CONSTRAINTS==
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|PDB= 1a56 |SIZE=350|CAPTION= <scene name='initialview01'>1a56</scene>
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<StructureSection load='1a56' size='340' side='right'caption='[[1a56]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>
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<table><tr><td colspan='2'>[[1a56]] 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=1A56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A56 FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE=
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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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|DOMAIN=
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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=1a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a56 OCA], [https://pdbe.org/1a56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a56 RCSB], [https://www.ebi.ac.uk/pdbsum/1a56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a56 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a56 OCA], [http://www.ebi.ac.uk/pdbsum/1a56 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a56 RCSB]</span>
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== Function ==
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}}
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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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'''PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERRICYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITH EXPLICIT HYDROGEN BOND CONSTRAINTS'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/1a56_consurf.spt"</scriptWhenChecked>
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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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<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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==About this Structure==
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</jmolCheckbox>
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1A56 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A56 OCA].
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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=1a56 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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://www.ncbi.nlm.nih.gov/pubmed/9746537 9746537]
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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: cytochrome]]
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[[Category: hemoprotein]]
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[[Category: prokaryotic electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:31 2008''
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Current revision

PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERRICYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITH EXPLICIT HYDROGEN BOND CONSTRAINTS

PDB ID 1a56

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