2b08

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[[Image:2b08.gif|left|200px]]
 
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{{Structure
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==Reduced acetamide-bound M150G Nitrite Reductase from Alcaligenes faecalis==
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|PDB= 2b08 |SIZE=350|CAPTION= <scene name='initialview01'>2b08</scene>, resolution 1.90&Aring;
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<StructureSection load='2b08' size='340' side='right'caption='[[2b08]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>
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<table><tr><td colspan='2'>[[2b08]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B08 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE= nirK, nir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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=2b08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b08 OCA], [https://pdbe.org/2b08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b08 RCSB], [https://www.ebi.ac.uk/pdbsum/2b08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b08 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=2b08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b08 OCA], [http://www.ebi.ac.uk/pdbsum/2b08 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b08 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/NIR_ALCFA NIR_ALCFA]
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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/b0/2b08_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=2b08 ConSurf].
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<div style="clear:both"></div>
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'''Reduced acetamide-bound M150G Nitrite Reductase from Alcaligenes faecalis'''
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==See Also==
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*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Copper-containing nitrite reductase harbors a type-1 and a type-2 Cu site. The former acts as the electron acceptor site of the enzyme, and the latter is the site of catalytic action. The effect of the methionine ligand on the reorganization energy of the type-1 site was explored by studying the electron-transfer kinetics between NiR (wild type (wt) and the variants Met150Gly and Met150Thr) with Fe(II)EDTA and Fe(II)HEDTA. The mutations increased the reorganization energy by 0.3 eV (30 kJ mol-1). A similar increase was found from pulse radiolysis experiments on the wt NIR and three variants (Met150Gly, Met150His, and Met150Thr). Binding of the nearby Met62 to the type-1 Cu site in Met150Gly (under influence of an allosteric effector) lowered the reorganization energy back to approximately the wt value. According to XRD data the structure of the reduced type-1 site in Met150Gly NiR in the presence of an allosteric effector is similar to that in the reduced wt NiR (solved to 1.85 A), compatible with the similarity in reorganization energy.
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==About this Structure==
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2B08 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B08 OCA].
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==Reference==
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Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase., Wijma HJ, MacPherson I, Farver O, Tocheva EI, Pecht I, Verbeet MP, Murphy ME, Canters GW, J Am Chem Soc. 2007 Jan 24;129(3):519-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17227014 17227014]
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[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
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[[Category: Nitrite reductase (NO-forming)]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Canters GW]]
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[[Category: Canters, G W.]]
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[[Category: Farver O]]
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[[Category: Farver, O.]]
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[[Category: MacPherson IS]]
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[[Category: MacPherson, I S.]]
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[[Category: Murphy MEP]]
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[[Category: Murphy, M E.P.]]
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[[Category: Pecht I]]
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[[Category: Pecht, I.]]
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[[Category: Tocheva EI]]
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[[Category: Tocheva, E I.]]
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[[Category: Verbeet MPh]]
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[[Category: Verbeet, M Ph.]]
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[[Category: Wijma HJ]]
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[[Category: Wijma, H J.]]
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[[Category: acetamide]]
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[[Category: allosteric control]]
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[[Category: axial methionine]]
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[[Category: met62]]
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[[Category: reorganization energy]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:59:44 2008''
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Current revision

Reduced acetamide-bound M150G Nitrite Reductase from Alcaligenes faecalis

PDB ID 2b08

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