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3wt4

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Revision as of 07:12, 23 December 2016

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

Structural highlights

3wt4 is a 4 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4njq, 4oid, 4oiw
Gene:	apeB, PA3247 (PSEAE)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The peptidases in clan MH are known as cocatalytic zinc peptidases that have two zinc ions in the active site, but their metal preference has not been rigorously investigated. In this study, the molecular basis for metal preference is provided from the structural and biochemical analyses. Kinetic studies of Pseudomonas aeruginosa aspartyl aminopeptidase (PaAP) which belongs to peptidase family M18 in clan MH revealed that its peptidase activity is dependent on Co2+ rather than Zn2+: the kcat (s-1) values of PaAP were 0.006, 5.10 and 0.43 in no-metal, Co2+, and Zn2+conditions, respectively. Consistently, addition of low concentrations of Co2+ to PaAP previously saturated with Zn2+ greatly enhanced the enzymatic activity, suggesting that Co2+may be the physiologically relevant cocatalytic metal ion of PaAP. The crystal structures of PaAP complexes with Co2+ or Zn2+ commonly showed two metal ions in the active site coordinated with three conserved residues and a bicarbonate ion in a tetragonal geometry. However, Co2+- and Zn2+-bound structures showed no noticeable alterations relevant to differential effects of metal species, except the relative orientation of Glu-265, a general base in the active site. The characterization of mutant PaAP revealed that the first metal binding site is primarily responsible for metal preference. Similar to PaAP, Streptococcus pneumonia glutamyl aminopeptidase (SpGP), belonging to aminopeptidase family M42 in clan MH, also showed requirement for Co2+ for maximum activity. These results proposed that clan MH peptidases might be a cocatalytic cobalt peptidase rather than a zinc-dependent peptidase.

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa.,Nguyen DD, Pandian R, Kim D, Ha SC, Yoon HJ, Kim KS, Yun KH, Kim JH, Kim KK Biochem Biophys Res Commun. 2014 Apr 1. pii: S0006-291X(14)00561-0. doi:, 10.1016/j.bbrc.2014.03.109. PMID:24704201^[1]

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

References

↑ Nguyen DD, Pandian R, Kim D, Ha SC, Yoon HJ, Kim KS, Yun KH, Kim JH, Kim KK. Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa. Biochem Biophys Res Commun. 2014 Apr 1. pii: S0006-291X(14)00561-0. doi:, 10.1016/j.bbrc.2014.03.109. PMID:24704201 doi:http://dx.doi.org/10.1016/j.bbrc.2014.03.109

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3wt4"

@@ Line 1: / Line 1: @@
 ==Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa==
 <StructureSection load='3wt4' size='340' side='right' caption='[[3wt4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4njq|4njq]], [[4oid|4oid]], [[4oiw|4oiw]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apeB, PA3247 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=3wt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wt4 RCSB], [http://www.ebi.ac.uk/pdbsum/3wt4 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=3wt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wt4 OCA], [http://pdbe.org/3wt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wt4 RCSB], [http://www.ebi.ac.uk/pdbsum/3wt4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wt4 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3wt4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3wt4

From Proteopedia

Revision as of 07:12, 23 December 2016

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

Structural highlights

Publication Abstract from PubMed

References

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