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5e3x

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Crystal structure of thermostable Carboxypeptidase (FisCP) from Fervidobacterium Islandicum AW-1

Structural highlights

5e3x is a 1 chain structure with sequence from Fervidobacterium islandicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.197Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A140UHP3_FERIS Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.[PIRNR:PIRNR006615]

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^[1]

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

References

↑ Lee YJ, Dhanasingh I, Ahn JS, Jin HS, Choi JM, Lee SH, Lee DW. Biochemical and structural characterization of a keratin-degrading M32 carboxypeptidase from Fervidobacterium islandicum AW-1. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2015.11.058

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5e3x"

@@ Line 1: / Line 1: @@
 ==Crystal structure of thermostable Carboxypeptidase (FisCP) from Fervidobacterium Islandicum AW-1==
-<StructureSection load='5e3x' size='340' side='right' caption='[[5e3x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='5e3x' size='340' side='right'caption='[[5e3x]], [[Resolution|resolution]] 2.20&Aring;' 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>
+<table><tr><td colspan='2'>[[5e3x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fervidobacterium_islandicum Fervidobacterium islandicum]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.197&#8491;</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>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e3x OCA], [https://pdbe.org/5e3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e3x RCSB], [https://www.ebi.ac.uk/pdbsum/5e3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e3x ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A140UHP3_FERIS A0A140UHP3_FERIS] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.[PIRNR:PIRNR006615]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 19: @@
 </div>
 <div class="pdbe-citations 5e3x" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Dhanasingh, I]]
+[[Category: Fervidobacterium islandicum]]
-[[Category: Lee, D W]]
+[[Category: Large Structures]]
-[[Category: Lee, S H]]
+[[Category: Dhanasingh I]]
-[[Category: Lee, Y J]]
+[[Category: Lee DW]]
-[[Category: Carboxypeptidase]]
+[[Category: Lee SH]]
-[[Category: Fervidobacterium]]
+[[Category: Lee Y-J]]
-[[Category: Fiscp]]
-[[Category: Hydrolase]]

5e3x

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Current revision

Crystal structure of thermostable Carboxypeptidase (FisCP) from Fervidobacterium Islandicum AW-1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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