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4azu

From Proteopedia

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(New page: 200px<br /><applet load="4azu" size="450" color="white" frame="true" align="right" spinBox="true" caption="4azu, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE ANA...)
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[[Image:4azu.gif|left|200px]]<br /><applet load="4azu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4azu, resolution 1.9&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF OXIDIZED PSEUDOMONAS AERUGINOSA AZURIN AT PH 5.5 AND PH 9.0. A PH-INDUCED CONFORMATIONAL TRANSITION INVOLVES A PEPTIDE BOND FLIP'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF OXIDIZED PSEUDOMONAS AERUGINOSA AZURIN AT PH 5.5 AND PH 9.0. A PH-INDUCED CONFORMATIONAL TRANSITION INVOLVES A PEPTIDE BOND FLIP==
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The X-ray crystal structure of recombinant wild-type azurin from, Pseudomonas aeruginosa was determined by difference Fourier techniques, using phases derived from the structure of the mutant His35Leu. Two data, sets were collected from a single crystal of oxidized azurin soaked in, mother liquor buffered at pH 5.5 and pH 9.0, respectively. Both data sets, extend to 1.93 A resolution. The two pH forms were refined independently, to crystallographic R-factors of 17.6% (pH 5.5) and 17.5% (pH 9.0). The, conformational transition previously attributed to the, protonation/deprotonation of residue His35 (pKa(red) = 7.3, pKa(ox) =, 6.2), which lies in a crevice of the protein close to the copper binding, site, involves a concomitant Pro36-Gly37 main-chain peptide bond flip. At, the lower pH, the protonated imidazole N delta 1 of His35 forms a strong, hydrogen bond with the carbonyl oxygen from Pro36, while at alkaline pH, the deprotonated N delta 1 acts as an acceptor of a weak hydrogen bond, from HN Gly37. The structure of the remainder of the azurin molecule, including the copper binding site, is not significantly affected by this, transition.
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<StructureSection load='4azu' size='340' side='right'caption='[[4azu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4azu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AZU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4azu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azu OCA], [http://pdbe.org/4azu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4azu RCSB], [http://www.ebi.ac.uk/pdbsum/4azu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4azu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome 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/az/4azu_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=4azu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The X-ray crystal structure of recombinant wild-type azurin from Pseudomonas aeruginosa was determined by difference Fourier techniques using phases derived from the structure of the mutant His35Leu. Two data sets were collected from a single crystal of oxidized azurin soaked in mother liquor buffered at pH 5.5 and pH 9.0, respectively. Both data sets extend to 1.93 A resolution. The two pH forms were refined independently to crystallographic R-factors of 17.6% (pH 5.5) and 17.5% (pH 9.0). The conformational transition previously attributed to the protonation/deprotonation of residue His35 (pKa(red) = 7.3, pKa(ox) = 6.2), which lies in a crevice of the protein close to the copper binding site, involves a concomitant Pro36-Gly37 main-chain peptide bond flip. At the lower pH, the protonated imidazole N delta 1 of His35 forms a strong hydrogen bond with the carbonyl oxygen from Pro36, while at alkaline pH the deprotonated N delta 1 acts as an acceptor of a weak hydrogen bond from HN Gly37. The structure of the remainder of the azurin molecule, including the copper binding site, is not significantly affected by this transition.
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==About this Structure==
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Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip.,Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW J Mol Biol. 1991 Oct 5;221(3):765-72. PMID:1942029<ref>PMID:1942029</ref>
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4AZU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU and NO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4AZU OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip., Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW, J Mol Biol. 1991 Oct 5;221(3):765-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1942029 1942029]
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</div>
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[[Category: Pseudomonas aeruginosa]]
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<div class="pdbe-citations 4azu" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Huber, R.]]
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[[Category: Messerschmidt, A.]]
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[[Category: Nar, H.]]
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[[Category: CU]]
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[[Category: NO3]]
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[[Category: electron transport(copper binding)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:25:48 2007''
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==See Also==
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*[[Azurin|Azurin]]
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*[[Intramolecular Electron Transfer in Azurin|Intramolecular Electron Transfer in Azurin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Huber, R]]
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[[Category: Messerschmidt, A]]
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[[Category: Nar, H]]

Current revision

CRYSTAL STRUCTURE ANALYSIS OF OXIDIZED PSEUDOMONAS AERUGINOSA AZURIN AT PH 5.5 AND PH 9.0. A PH-INDUCED CONFORMATIONAL TRANSITION INVOLVES A PEPTIDE BOND FLIP

PDB ID 4azu

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