1rcy

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[[Image:1rcy.gif|left|200px]]<br /><applet load="1rcy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rcy, resolution 1.9&Aring;" />
 
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'''RUSTICYANIN (RC) FROM THIOBACILLUS FERROOXIDANS'''<br />
 
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==Overview==
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==RUSTICYANIN (RC) FROM THIOBACILLUS FERROOXIDANS==
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The X-ray crystal structure of the oxidized form of the extremely stable, and highly oxidizing cupredoxin rusticyanin from Thiobacillus ferrooxidans, has been determined by the method of multiwavelength anomalous diffraction, (MAD) and refined to 1.9 A resolution. Like other cupredoxins, rusticyanin, is a copper-containing metalloprotein, which is composed of a core, beta-sandwich fold. In rusticyanin the beta-sandwich is composed of a six-, and a seven-stranded beta-sheet. Also like other cupredoxins, the copper, ion is coordinated by a cluster of four conserved residues (His85, Cys138, His143, Met148) arranged in a distorted tetrahedron. Rusticyanin has a, redox potential of 680 mV, roughly twice that of any other cupredoxin, and, it is optimally active at pH values &lt; or = 2. By comparison with other, cupredoxins, the three-dimensional structure of rusticyanin reveals, several possible sources of the chemical differences, including more, ordered secondary structure and more intersheet connectivity than other, cupredoxins. The acid stability and redox potential of rusticyanin may, also be enhanced over other cupredoxins by a more extensive internal, hydrogen bonding network and by more extensive hydrophobic interactions, surrounding the copper binding site. Finally, reduction in the number of, charged residues surrounding the active site may also make a major, contribution to acid stability. We propose that the resulting rigid copper, binding site, which is constrained by the surrounding hydrophobic, environment, structurally and electronically favours Cu(I). We propose, that the two extreme chemical properties of rusticyanin are interrelated;, the same unique structural features that enhance acid stability also lead, to elevated redox potential.
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<StructureSection load='1rcy' size='340' side='right'caption='[[1rcy]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1rcy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RCY FirstGlance]. <br>
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1RCY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=ASI:Distorted Tetrahedral Coordination By 2 HIS, 1 CYS, And ...'>ASI</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RCY OCA].
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=1rcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rcy OCA], [https://pdbe.org/1rcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rcy RCSB], [https://www.ebi.ac.uk/pdbsum/1rcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rcy ProSAT]</span></td></tr>
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Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: a highly oxidizing cupredoxin with extreme acid stability., Walter RL, Ealick SE, Friedman AM, Blake RC 2nd, Proctor P, Shoham M, J Mol Biol. 1996 Nov 15;263(5):730-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8947572 8947572]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RUS2_ACIFI RUS2_ACIFI] Electron carrier from cytochrome c552 to the A-type oxidase.
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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/rc/1rcy_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=1rcy ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Acidithiobacillus ferrooxidans]]
[[Category: Acidithiobacillus ferrooxidans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ealick, S.E.]]
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[[Category: Blake II RC]]
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[[Category: Friedman, A.M.]]
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[[Category: Ealick SE]]
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[[Category: II, R.C.Blake.]]
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[[Category: Friedman AM]]
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[[Category: Proctor, P.]]
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[[Category: Proctor P]]
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[[Category: Shoham, M.]]
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[[Category: Shoham M]]
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[[Category: Walter, R.L.]]
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[[Category: Walter RL]]
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[[Category: CU]]
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[[Category: copper containing protein]]
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[[Category: metalloprotein]]
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[[Category: oxidation potential]]
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[[Category: ph stability]]
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[[Category: redox protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:59:09 2007''
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Current revision

RUSTICYANIN (RC) FROM THIOBACILLUS FERROOXIDANS

PDB ID 1rcy

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