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| | <StructureSection load='2wwt' size='340' side='right'caption='[[2wwt]], [[Resolution|resolution]] 2.68Å' scene=''> | | <StructureSection load='2wwt' size='340' side='right'caption='[[2wwt]], [[Resolution|resolution]] 2.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wwt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700160 Atcc 700160]. 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://proteopedia.org/fgij/fg.htm?mol=2WWT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wwt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_clausii Alkalihalobacillus 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 [https://proteopedia.org/fgij/fg.htm?mol=2WWT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.68Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wv7|2wv7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2wwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wwt OCA], [https://pdbe.org/2wwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wwt RCSB], [https://www.ebi.ac.uk/pdbsum/2wwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wwt ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wwt OCA], [http://pdbe.org/2wwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wwt RCSB], [http://www.ebi.ac.uk/pdbsum/2wwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wwt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D0AB41_ALKCL D0AB41_ALKCL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 700160]] | + | [[Category: Alkalihalobacillus clausii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]]
| + | [[Category: Ariza A]] |
| - | [[Category: Ariza, A]] | + | [[Category: Dodson E]] |
| - | [[Category: Dodson, E]] | + | [[Category: Gamble M]] |
| - | [[Category: Gamble, M]] | + | [[Category: Jones DD]] |
| - | [[Category: Jones, D D]] | + | [[Category: Vevodova J]] |
| - | [[Category: Vevodova, J]] | + | [[Category: Wilson KS]] |
| - | [[Category: Wilson, K S]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Intracellular proteinase regulation]]
| + | |
| Structural highlights
Function
D0AB41_ALKCL
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
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vevodova J, Gamble M, Kunze G, Ariza A, Dodson E, Jones DD, Wilson KS. Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family. Structure. 2010 Jun 9;18(6):744-55. PMID:20541512 doi:10.1016/j.str.2010.03.008
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