1zds

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(New page: 200px<br /><applet load="1zds" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zds, resolution 1.55&Aring;" /> '''Crystal Structure of...)
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[[Image:1zds.gif|left|200px]]<br /><applet load="1zds" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zds, resolution 1.55&Aring;" />
 
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'''Crystal Structure of Met150Gly AfNiR with Acetamide Bound'''<br />
 
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==Overview==
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==Crystal Structure of Met150Gly AfNiR with Acetamide Bound==
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In Cu-containing nitrite reductase from Alcaligenes faecalis S-6 the axial, methionine ligand of the type-1 site was replaced (M150G) to make the, copper ion accessible to external ligands that might affect the enzyme's, catalytic activity. The type-1 site optical spectrum of M150G, (A(460)/A(600)=0.71) differs significantly from that of the native nitrite, reductase (A(460)/A(600)=1.3). The midpoint potential of the type-1 site, of nitrite reductase M150G (E(M)=312(+/-5)mV versus hydrogen) is higher, than that of the native enzyme (E(M)=213(+/-5)mV). M150G has a lower, catalytic activity (k(cat)=133(+/-6)s(-1)) than the wild-type nitrite, reductase (k(cat)=416(+/-10)s(-1)). The binding of external ligands to, M150G restores spectral properties, midpoint potential (E(M)&lt;225mV), and, catalytic activity (k(cat)=374(+/-28)s(-1)). Also the M150H, (A(460)/A(600)=7.7, E(M)=104(+/-5)mV, k(cat)=0.099(+/-0.006)s(-1)) and, M150T (A(460)/A(600)=0.085, E(M)=340(+/-5)mV, k(cat)=126(+/-2)s(-1)), variants were characterized. Crystal structures show that the ligands act, as allosteric effectors by displacing Met62, which moves to bind to the Cu, in the position emptied by the M150G mutation. The reconstituted type-1, site has an otherwise unaltered geometry. The observation that removal of, an endogenous ligand can introduce allosteric control in a redox enzyme, suggests potential for structural and functional flexibility of, copper-containing redox sites.
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<StructureSection load='1zds' size='340' side='right'caption='[[1zds]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zds]] 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=1ZDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZDS FirstGlance]. <br>
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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]] 1.55&#8491;</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=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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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=1zds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zds OCA], [https://pdbe.org/1zds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zds RCSB], [https://www.ebi.ac.uk/pdbsum/1zds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zds ProSAT]</span></td></tr>
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</table>
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== Function ==
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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/zd/1zds_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=1zds ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ZDS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with CU and ACM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZDS OCA].
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*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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A rearranging ligand enables allosteric control of catalytic activity in copper-containing nitrite reductase., Wijma HJ, Macpherson I, Alexandre M, Diederix RE, Canters GW, Murphy ME, Verbeet MP, J Mol Biol. 2006 May 12;358(4):1081-93. Epub 2006 Mar 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16574144 16574144]
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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: Alexandre M]]
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[[Category: Alexandre, M.]]
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[[Category: Canters GW]]
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[[Category: Canters, G.W.]]
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[[Category: Diederix REM]]
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[[Category: Diederix, R.E.M.]]
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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: Verbeet MP]]
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[[Category: Verbeet, M.P.]]
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[[Category: Wijma HJ]]
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[[Category: Wijma, H.J.]]
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[[Category: ACM]]
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[[Category: CU]]
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[[Category: metal-binding]]
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[[Category: nitrate assimiliation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:24:29 2007''
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Current revision

Crystal Structure of Met150Gly AfNiR with Acetamide Bound

PDB ID 1zds

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