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| | <StructureSection load='1r64' size='340' side='right'caption='[[1r64]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1r64' size='340' side='right'caption='[[1r64]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r64]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R64 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R64 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r64]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R64 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.2Å</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>, <scene name='pdbligand=BOR:(1R)-1-AMINO-4-{[(E)-AMINO(IMINO)METHYL]AMINO}BUTYLBORONIC+ACID'>BOR</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=BOR:(1R)-1-AMINO-4-{[(E)-AMINO(IMINO)METHYL]AMINO}BUTYLBORONIC+ACID'>BOR</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KEX2 OR QDS1 OR YNL238W OR N1122 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1r64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r64 OCA], [https://pdbe.org/1r64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r64 RCSB], [https://www.ebi.ac.uk/pdbsum/1r64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r64 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Kexin Kexin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.61 3.4.21.61] </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=1r64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r64 OCA], [http://pdbe.org/1r64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r64 RCSB], [http://www.ebi.ac.uk/pdbsum/1r64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r64 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KEX2_YEAST KEX2_YEAST]] Processing of precursors of alpha-factors and killer toxin. | + | [https://www.uniprot.org/uniprot/KEX2_YEAST KEX2_YEAST] Processing of precursors of alpha-factors and killer toxin. |
| | == 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 18824]] | |
| - | [[Category: Kexin]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fuller, R S]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Holyoak, T]] | + | [[Category: Fuller RS]] |
| - | [[Category: Kettner, C A]] | + | [[Category: Holyoak T]] |
| - | [[Category: Petsko, G A]] | + | [[Category: Kettner CA]] |
| - | [[Category: Ringe, D]] | + | [[Category: Petsko GA]] |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | [[Category: Ringe D]] |
| - | [[Category: Kex2]]
| + | |
| - | [[Category: Prohormone processing]]
| + | |
| - | [[Category: Proprotein convertase]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Protein convertase]]
| + | |
| - | [[Category: Subtilisin]]
| + | |
| Structural highlights
1r64 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.2Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
KEX2_YEAST Processing of precursors of alpha-factors and killer toxin.
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
Kex2 is the yeast prototype of a large family of serine proteases that are highly specific for cleavage of their peptide substrates C-terminal to paired basic sites. This paper reports the 2.2 A resolution crystal structure of ssKex2 in complex with an Ac-Arg-Glu-Lys-Arg peptidyl boronic acid inhibitor (R = 19.7, R(free) = 23.4). By comparison of this structure with the structure of the mammalian homologue furin [Henrich, S., et al. (2003) Nat. Struct. Biol. 10, 520-526], we suggest a structural basis for the differences in substrate recognition at the P(2) and P(4) positions between Kex2 and furin and provide a structural rationale for the lack of P(6) recognition in Kex2. In addition, several monovalent cation binding sites are identified, and a mechanism of activation of Kex2 by potassium ion is proposed.
Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases.,Holyoak T, Kettner CA, Petsko GA, Fuller RS, Ringe D Biochemistry. 2004 Mar 9;43(9):2412-21. PMID:14992578[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Holyoak T, Kettner CA, Petsko GA, Fuller RS, Ringe D. Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases. Biochemistry. 2004 Mar 9;43(9):2412-21. PMID:14992578 doi:10.1021/bi035849h
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