1ac5

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Revision as of 09:21, 9 August 2017

CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE

Structural highlights

1ac5 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Carboxypeptidase D, with EC number 3.4.16.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KEX1_YEAST] Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11]

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

Kex1p is a prohormone-processing serine carboxypeptidase found in Saccharomyces cerevisiae. In contrast to yeast serine carboxypeptidase (CPD-Y) and wheat serine carboxypeptidase II (CPDW-II), Kex1p displays a very narrow specificity for lysyl or arginyl residues at the C-terminus of the substrate. The structure of Kex1Deltap, an enzyme that lacks the acidic domain and membrane-spanning portion of Kex1p, has been solved by a combination of molecular replacement and multiple isomorphous replacement and refined to a resolution of 2.4 A. The S1' site of Kex1Deltap is sterically restricted compared to those from CPD-Y or CPDW-II; it also contains two acidic groups that are well positioned to interact with the basic group of a lysine or arginine side chain. The high specificity of Kex1p can therefore be explained by a combination of steric and electronic factors. The structure of the S1 site of Kex1Deltap is also well suited for binding of a lysine or arginine side chain, and the enzyme may therefore exhibit a preference for these residues at P1.

Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae,.,Shilton BH, Thomas DY, Cygler M Biochemistry. 1997 Jul 22;36(29):9002-12. PMID:9220988^[12]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dmochowska A, Dignard D, Henning D, Thomas DY, Bussey H. Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing. Cell. 1987 Aug 14;50(4):573-84. PMID:3301004
↑ Wickner RB. Chromosomal and nonchromosomal mutations affecting the "killer character" of Saccharomyces cerevisiae. Genetics. 1974 Mar;76(3):423-32. PMID:4364866
↑ Wickner RB, Leibowitz MJ. Two chromosomal genes required for killing expression in killer strains of Saccharomyces cerevisiae. Genetics. 1976 Mar 25;82(3):429-42. PMID:773743
↑ Wagner JC, Wolf DH. Hormone (pheromone) processing enzymes in yeast. The carboxy-terminal processing enzyme of the mating pheromone alpha-factor, carboxypeptidase ysc alpha, is absent in alpha-factor maturation-defective kex1 mutant cells. FEBS Lett. 1987 Sep 14;221(2):423-6. PMID:3305079
↑ Zhu H, Bussey H, Thomas DY, Gagnon J, Bell AW. Determination of the carboxyl termini of the alpha and beta subunits of yeast K1 killer toxin. Requirement of a carboxypeptidase B-like activity for maturation. J Biol Chem. 1987 Aug 5;262(22):10728-32. PMID:3301840
↑ Cooper A, Bussey H. Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane. J Cell Biol. 1992 Dec;119(6):1459-68. PMID:1469044
↑ Latchinian-Sadek L, Thomas DY. Expression, purification, and characterization of the yeast KEX1 gene product, a polypeptide precursor processing carboxypeptidase. J Biol Chem. 1993 Jan 5;268(1):534-40. PMID:8416959
↑ Eisfeld K, Riffer F, Mentges J, Schmitt MJ. Endocytotic uptake and retrograde transport of a virally encoded killer toxin in yeast. Mol Microbiol. 2000 Aug;37(4):926-40. PMID:10972812
↑ Riffer F, Eisfeld K, Breinig F, Schmitt MJ. Mutational analysis of K28 preprotoxin processing in the yeast Saccharomyces cerevisiae. Microbiology. 2002 May;148(Pt 5):1317-28. PMID:11988505
↑ Heiman MG, Engel A, Walter P. The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating. J Cell Biol. 2007 Jan 15;176(2):209-22. Epub 2007 Jan 8. PMID:17210951 doi:http://dx.doi.org/jcb.200609182
↑ Hauptmann P, Lehle L. Kex1 protease is involved in yeast cell death induced by defective N-glycosylation, acetic acid, and chronological aging. J Biol Chem. 2008 Jul 4;283(27):19151-63. doi: 10.1074/jbc.M801303200. Epub 2008 , May 12. PMID:18474590 doi:http://dx.doi.org/10.1074/jbc.M801303200
↑ Shilton BH, Thomas DY, Cygler M. Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae,. Biochemistry. 1997 Jul 22;36(29):9002-12. PMID:9220988 doi:http://dx.doi.org/10.1021/bi970433n

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ac5"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE==
 <StructureSection load='1ac5' size='340' side='right' caption='[[1ac5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_D Carboxypeptidase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.6 3.4.16.6] </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=1ac5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac5 OCA], [http://pdbe.org/1ac5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ac5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ac5 PDBsum]</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=1ac5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac5 OCA], [http://pdbe.org/1ac5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ac5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ac5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ac5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <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].
+</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=1ac5 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1ac5

From Proteopedia

Revision as of 09:21, 9 August 2017

CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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