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| - | [[Image:5pal.gif|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURE OF THE UNIQUE PARVALBUMIN COMPONENT FROM MUSCLE OF THE LEOPARD SHARK (TRIAKIS SEMIFASCIATA). THE FIRST X-RAY STUDY OF AN ALPHA-PARVALBUMIN== |
| - | |PDB= 5pal |SIZE=350|CAPTION= <scene name='initialview01'>5pal</scene>, resolution 1.54Å
| + | <StructureSection load='5pal' size='340' side='right'caption='[[5pal]], [[Resolution|resolution]] 1.54Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | <table><tr><td colspan='2'>[[5pal]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triakis_semifasciata Triakis semifasciata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5PAL FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</td></tr> |
| - | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5pal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5pal OCA], [https://pdbe.org/5pal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5pal RCSB], [https://www.ebi.ac.uk/pdbsum/5pal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5pal ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5pal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5pal OCA], [http://www.ebi.ac.uk/pdbsum/5pal PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5pal RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/PRVA_TRISE PRVA_TRISE] 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/pa/5pal_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=5pal ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE UNIQUE PARVALBUMIN COMPONENT FROM MUSCLE OF THE LEOPARD SHARK (TRIAKIS SEMIFASCIATA). THE FIRST X-RAY STUDY OF AN ALPHA-PARVALBUMIN'''
| + | ==See Also== |
| - | | + | *[[Parvalbumin|Parvalbumin]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | The three-dimensional structure of parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark parvalbumin shows the main features of all parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-parvalbumin higher in comparison to that of a beta-parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark parvalbumin, as in nearly all alpha-parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
| + | [[Category: Large Structures]] |
| - | | + | |
| - | ==About this Structure==
| + | |
| - | 5PAL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Triakis_semifasciata Triakis semifasciata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PAL OCA].
| + | |
| - | | + | |
| - | ==Reference==
| + | |
| - | Crystal structure of the unique parvalbumin component from muscle of the leopard shark (Triakis semifasciata). The first X-ray study of an alpha-parvalbumin., Roquet F, Declercq JP, Tinant B, Rambaud J, Parello J, J Mol Biol. 1992 Feb 5;223(3):705-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1542115 1542115]
| + | |
| - | [[Category: Single protein]] | + | |
| | [[Category: Triakis semifasciata]] | | [[Category: Triakis semifasciata]] |
| - | [[Category: Declercq, J P.]] | + | [[Category: Declercq J-P]] |
| - | [[Category: Parello, J.]] | + | [[Category: Parello J]] |
| - | [[Category: Rambaud, J.]] | + | [[Category: Rambaud J]] |
| - | [[Category: Roquet, F.]] | + | [[Category: Roquet F]] |
| - | [[Category: Tinant, B.]] | + | [[Category: Tinant B]] |
| - | [[Category: calcium-binding protein]]
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| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:42:01 2008''
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