1r64

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(New page: 200px<br /><applet load="1r64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r64, resolution 2.20&Aring;" /> '''The 2.2 A crystal st...)
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[[Image:1r64.jpg|left|200px]]<br /><applet load="1r64" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1r64, resolution 2.20&Aring;" />
 
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'''The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor'''<br />
 
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==Overview==
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==The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor==
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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.
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<StructureSection load='1r64' size='340' side='right'caption='[[1r64]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KEX2_YEAST KEX2_YEAST] Processing of precursors of alpha-factors and killer toxin.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r6/1r64_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1r64 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:14992578</ref>
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1R64 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAG, CA, K, ACE and BTB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R64 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14992578 14992578]
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</div>
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[[Category: Kexin]]
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<div class="pdbe-citations 1r64" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Fuller RS]]
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[[Category: Fuller, R.S.]]
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[[Category: Holyoak T]]
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[[Category: Holyoak, T.]]
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[[Category: Kettner CA]]
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[[Category: Kettner, C.A.]]
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[[Category: Petsko GA]]
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[[Category: Petsko, G.A.]]
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[[Category: Ringe D]]
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[[Category: Ringe, D.]]
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[[Category: ACE]]
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[[Category: BTB]]
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[[Category: CA]]
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[[Category: K]]
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[[Category: NAG]]
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[[Category: kex2]]
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[[Category: kexin]]
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[[Category: prohormone processing]]
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[[Category: proprotein convertase]]
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[[Category: protease]]
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[[Category: protein convertase]]
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[[Category: subtilisin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:17:51 2007''
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Current revision

The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor

PDB ID 1r64

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