|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1c3l' size='340' side='right'caption='[[1c3l]], [[Resolution|resolution]] 2.16Å' scene=''> | | <StructureSection load='1c3l' size='340' side='right'caption='[[1c3l]], [[Resolution|resolution]] 2.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1c3l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C3L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1c3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C3L 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>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=XE:XENON'>XE</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]] 2.16Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sbc|1sbc]], [[1bfu|1bfu]], [[1bfk|1bfk]], [[1sca|1sca]], [[1av7|1av7]], [[1avt|1avt]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=XE:XENON'>XE</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=1c3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3l OCA], [https://pdbe.org/1c3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c3l RCSB], [https://www.ebi.ac.uk/pdbsum/1c3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c3l ProSAT]</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=1c3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3l OCA], [http://pdbe.org/1c3l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c3l RCSB], [http://www.ebi.ac.uk/pdbsum/1c3l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c3l ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUBT_BACLI SUBT_BACLI]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. | + | [https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Subtilisin|Subtilisin]] | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 39: |
Line 38: |
| | [[Category: Bacillus licheniformis]] | | [[Category: Bacillus licheniformis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Longhi, S]] | + | [[Category: Longhi S]] |
| - | [[Category: Pernot, L]] | + | [[Category: Pernot L]] |
| - | [[Category: Prange, T]] | + | [[Category: Prange T]] |
| - | [[Category: Schiltz, M]] | + | [[Category: Schiltz M]] |
| - | [[Category: H, N Colloc]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serine-proteinase]]
| + | |
| - | [[Category: Xenon]]
| + | |
| Structural highlights
Function
SUBC_BACLI Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).[1] [2]
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
X-ray diffraction is used to study the binding of xenon and krypton to a variety of crystallised proteins: porcine pancreatic elastase; subtilisin Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani; collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide dehydrogenase domain from the outer membrane protein P64k from Neisseria meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas pressures ranging from 8 to 20 bar, xenon is able to bind to discrete sites in hydrophobic cavities, ligand and substrate binding pockets, and into the pore of channel-like structures. These xenon complexes can be used to map hydrophobic sites in proteins, or as heavy-atom derivatives in the isomorphous replacement method of structure determination.
Exploring hydrophobic sites in proteins with xenon or krypton.,Prange T, Schiltz M, Pernot L, Colloc'h N, Longhi S, Bourguet W, Fourme R Proteins. 1998 Jan;30(1):61-73. PMID:9443341[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Evans KL, Crowder J, Miller ES. Subtilisins of Bacillus spp. hydrolyze keratin and allow growth on feathers. Can J Microbiol. 2000 Nov;46(11):1004-11. doi: 10.1139/w00-085. PMID:11109488 doi:http://dx.doi.org/10.1139/w00-085
- ↑ Smith EL, DeLange RJ, Evans WH, Landon M, Markland FS. Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships. J Biol Chem. 1968 May 10;243(9):2184-91. PMID:4967581
- ↑ Prange T, Schiltz M, Pernot L, Colloc'h N, Longhi S, Bourguet W, Fourme R. Exploring hydrophobic sites in proteins with xenon or krypton. Proteins. 1998 Jan;30(1):61-73. PMID:9443341
|
