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| | <StructureSection load='1bu3' size='340' side='right'caption='[[1bu3]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='1bu3' size='340' side='right'caption='[[1bu3]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Merluccius_bilinearis Merluccius bilinearis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BU3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Merluccius_bilinearis Merluccius bilinearis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BU3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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></td></tr> |
| - | <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=1bu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu3 OCA], [http://pdbe.org/1bu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1bu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu3 ProSAT]</span></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=1bu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu3 OCA], [https://pdbe.org/1bu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1bu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRVB_MERBI PRVB_MERBI]] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. | + | [https://www.uniprot.org/uniprot/PRVB_MERBI PRVB_MERBI] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1bu3_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1bu3_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Merluccius bilinearis]] | | [[Category: Merluccius bilinearis]] |
| - | [[Category: Harrington, D J]] | + | [[Category: Harrington DJ]] |
| - | [[Category: Nelson, D J]] | + | [[Category: Nelson DJ]] |
| - | [[Category: Richardson, R C]] | + | [[Category: Richardson RC]] |
| - | [[Category: Royer, W E]] | + | [[Category: Royer WE]] |
| - | [[Category: Calcium binding]]
| + | |
| Structural highlights
Function
PRVB_MERBI In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Parvalbumins constitute a class of calcium-binding proteins characterized by the presence of several helix-loop-helix (EF-hand) motifs. In a previous study (Revett SP, King G, Shabanowitz J, Hunt DF, Hartman KL, Laue TM, Nelson DJ, 1997, Protein Sci 7:2397-2408), we presented the sequence of the major parvalbumin isoform from the silver hake (Merluccius bilinearis) and presented spectroscopic and structural information on the excised "EF-hand" portion of the protein. In this study, the X-ray crystal structure of the silver hake major parvalbumin has been determined to high resolution, in the frozen state, using the molecular replacement method with the carp parvalbumin structure as a starting model. The crystals are orthorhombic, space group C2221, with a = 75.7 A, b = 80.7 A, and c = 42.1 A. Data were collected from a single crystal grown in 15% glycerol, which served as a cryoprotectant for flash freezing at -188 degrees C. The structure refined to a conventional R-value of 21% (free R 25%) for observed reflections in the range 8 to 1.65 A [1 > 2sigma(I)]. The refined model includes an acetylated amino terminus, 108 residues (characteristic of a beta parvalbumin lineage), 2 calcium ions, and 114 water molecules per protein molecule. The resulting structure was used in molecular dynamics (MD) simulations focused primarily on the dynamics of the ligands coordinating the Ca2+ ions in the CD and EF sites. MD simulations were performed on both the fully Ca2+ loaded protein and on a Ca2+ deficient variant, with Ca2+ only in the CD site. There was substantial agreement between the MD and X-ray results in addressing the issue of mobility of key residues in the calcium-binding sites, especially with regard to the side chain of Ser55 in the CD site and Asp92 in the EF site.
X-Ray crystal structure and molecular dynamics simulations of silver hake parvalbumin (Isoform B).,Richardson RC, King NM, Harrington DJ, Sun H, Royer WE, Nelson DJ Protein Sci. 2000 Jan;9(1):73-82. PMID:10739249[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Richardson RC, King NM, Harrington DJ, Sun H, Royer WE, Nelson DJ. X-Ray crystal structure and molecular dynamics simulations of silver hake parvalbumin (Isoform B). Protein Sci. 2000 Jan;9(1):73-82. PMID:10739249 doi:http://dx.doi.org/10.1110/ps.9.1.73
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