1pvb
From Proteopedia
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| - | [[Image:1pvb.jpg|left|200px]]<br /><applet load="1pvb" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1pvb, resolution 1.75Å" /> | ||
| - | '''X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN'''<br /> | ||
| - | == | + | ==X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN== |
| + | <StructureSection load='1pvb' size='340' side='right'caption='[[1pvb]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1pvb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Esox_lucius Esox lucius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PVB FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pvb OCA], [https://pdbe.org/1pvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pvb RCSB], [https://www.ebi.ac.uk/pdbsum/1pvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pvb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PRVB_ESOLU PRVB_ESOLU] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pv/1pvb_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1pvb ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I>/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell. | A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I>/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell. | ||
| - | + | X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.,Declercq JP, Tinant B, Parello J Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:15299738<ref>PMID:15299738</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1pvb" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Parvalbumin|Parvalbumin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Esox lucius]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Declercq JP]] | ||
| + | [[Category: Parello J]] | ||
| + | [[Category: Tinant B]] | ||
Current revision
X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN
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