5e3x: Difference between revisions
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''' | ==Crystal structure of thermostable Carboxypeptidase (FisCP) from Fervidobacterium Islandicum AW-1== | ||
<StructureSection load='5e3x' size='340' side='right' caption='[[5e3x]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5e3x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E3X FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></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=5e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e3x OCA], [http://pdbe.org/5e3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e3x RCSB], [http://www.ebi.ac.uk/pdbsum/5e3x PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Comparative genomics of the keratin-degrading extremophilic eubacterium Fervidobacterium islandicum AW-1 and the closely related Fervidobacterium nodosum with no keratinolytic activity suggested that the FIAW1_1600 gene encoding a carboxypeptidase (CP) plays an important role in keratin degradation. The presumptive 489 amino acid sequence of the gene showed a conserved HEXXH motif with low levels of sequence identity (<38%) to reported thermostable M32 CPs. To identify its functional role, the FIAW1_1600 gene was overexpressed in Escherichia coli, and the recombinant enzyme was purified and characterized in detail. F. islandicum AW-1 CP (FisCP) formed a homodimer with a molecular mass of 107 kDa, and its apoenzyme exhibited maximal activity at 80 degrees C and pH 7.0 in the presence of Co(2+). This metalloenzyme mainly cleaved the C-termini of peptides with a basic amino acid sequence. The crystal structure of FisCP at 2.2 A resolution showed high levels of structural similarities (root-mean-square deviations of <1.7 A) to those of other M32 CP homologs. Remarkably, the enzyme significantly enhanced the degradation of native chicken feathers. This study suggests that FisCP, a keratinolytic member of the thermostable M32 CP family, plays an important role in keratin degradation for cellular metabolism in F. islandicum AW-1. | |||
Biochemical and structural characterization of a keratin-degrading M32 carboxypeptidase from Fervidobacterium islandicum AW-1.,Lee YJ, Dhanasingh I, Ahn JS, Jin HS, Choi JM, Lee SH, Lee DW Biochem Biophys Res Commun. 2015 Dec 25;468(4):927-33. doi:, 10.1016/j.bbrc.2015.11.058. Epub 2015 Nov 19. PMID:26603937<ref>PMID:26603937</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5e3x" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dhanasingh, I]] | [[Category: Dhanasingh, I]] | ||
[[Category: Lee, D W]] | |||
[[Category: Lee, S H]] | |||
[[Category: Lee, Y J]] | |||
[[Category: Carboxypeptidase]] | |||
[[Category: Fervidobacterium]] | |||
[[Category: Fiscp]] | |||
[[Category: Hydrolase]] | |||
Revision as of 17:18, 10 February 2016
Crystal structure of thermostable Carboxypeptidase (FisCP) from Fervidobacterium Islandicum AW-1
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