2wwt
From Proteopedia
(Difference between revisions)
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| - | + | ==Intracellular subtilisin precursor from B. clausii== | |
| - | === | + | <StructureSection load='2wwt' size='340' side='right' caption='[[2wwt]], [[Resolution|resolution]] 2.68Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2wwt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_clausii Bacillus clausii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WWT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wv7|2wv7]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></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=2wwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wwt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wwt RCSB], [http://www.ebi.ac.uk/pdbsum/2wwt PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/ww/2wwt_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The intracellular subtilisin proteases (ISPs) are the only known members of the important and ubiquitous subtilisin family that function exclusively within the cell, constituting a major component of the degradome in many Gram-positive bacteria. The first ISP structure reported herein at a spacing of 1.56 A reveals features unique among subtilisins that has enabled potential functional and physiological roles to be assigned to sequence elements exclusive to the ISPs. Unlike all other subtilisins, ISP from B. clausii is dimeric, with residues from the C terminus making a major contribution to the dimer interface by crossing over to contact the partner subunit. A short N-terminal extension binds back across the active site to provide a potential novel regulatory mechanism of intrinsic proteolytic activity: a proline residue conserved throughout the ISPs introduces a kink in the polypeptide backbone that lifts the target peptide bond out of reach of the catalytic residues. | ||
| - | + | Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.,Vevodova J, Gamble M, Kunze G, Ariza A, Dodson E, Jones DD, Wilson KS Structure. 2010 Jun 9;18(6):744-55. PMID:20541512<ref>PMID:20541512</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Subtilisin|Subtilisin]] | *[[Subtilisin|Subtilisin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Bacillus clausii]] | [[Category: Bacillus clausii]] | ||
[[Category: Subtilisin]] | [[Category: Subtilisin]] | ||
| - | [[Category: Ariza, A | + | [[Category: Ariza, A]] |
| - | [[Category: Dodson, E | + | [[Category: Dodson, E]] |
| - | [[Category: Gamble, M | + | [[Category: Gamble, M]] |
| - | [[Category: Jones, D D | + | [[Category: Jones, D D]] |
| - | [[Category: Vevodova, J | + | [[Category: Vevodova, J]] |
| - | [[Category: Wilson, K S | + | [[Category: Wilson, K S]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Intracellular proteinase regulation]] | [[Category: Intracellular proteinase regulation]] | ||
Revision as of 17:53, 21 December 2014
Intracellular subtilisin precursor from B. clausii
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