1hlu
From Proteopedia
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- | [[Image:1hlu.png|left|200px]] | ||
- | + | ==STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE== | |
- | The | + | <StructureSection load='1hlu' size='340' side='right'caption='[[1hlu]], [[Resolution|resolution]] 2.65Å' scene=''> |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1hlu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The July 2001 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Actin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2001_7 10.2210/rcsb_pdb/mom_2001_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLU 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]] 2.65Å</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</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=1hlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlu OCA], [https://pdbe.org/1hlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hlu RCSB], [https://www.ebi.ac.uk/pdbsum/1hlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hlu ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ACTB_BOVIN ACTB_BOVIN] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | ||
+ | == 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/hl/1hlu_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=1hlu ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The structure of an "open state" of crystalline profilin:beta-actin has been solved to 2.65 A by X-ray crystallography. The open-state crystals, in 1.8 M potassium phosphate, have an expanded unit cell dimension in the c direction of 185.7 A compared with 171.9 A in the previously solved ammonium sulphate-stabilized "tight-state" structure. The unit cell change between the open and the tight states is accompanied by large subdomain movements in actin. Furthermore, the nucleotide in the open state is significantly more exposed to solvent, and local conformational changes in the hydrophobic pocket surrounding cysteine 374 occur during the transition to the tight state. Significant changes were observed at the N terminus and in the DNase-I binding loop. Neither the structure of profilin nor its contact with beta-actin are affected by the changes in the unit cell. Applying osmotic pressure to profilin:beta-actin crystals brings about a collapse of the unit cell comparable with that seen in the open to tight-state transition, enabling an estimate of the work required to cause this transformation of beta-actin in the crystals. The slight difference in energy between the open and collapsed states explains the extreme sensitivity of profilin:beta-actin crystals to changes in chemical and thermal environment. | ||
- | + | The structure of an open state of beta-actin at 2.65 A resolution.,Chik JK, Lindberg U, Schutt CE J Mol Biol. 1996 Nov 8;263(4):607-23. PMID:8918942<ref>PMID:8918942</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1hlu" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
- | *[[Actin]] | + | *[[Actin|Actin]] |
- | + | *[[Actin 3D structures|Actin 3D structures]] | |
- | == | + | *[[Profilin 3D Structures|Profilin 3D Structures]] |
- | < | + | == References == |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Actin]] | [[Category: Actin]] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
- | [[Category: Chik | + | [[Category: Chik JK]] |
- | [[Category: Lindberg | + | [[Category: Lindberg U]] |
- | [[Category: Schutt | + | [[Category: Schutt CE]] |
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Current revision
STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE
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