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2prq

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Revision as of 09:31, 18 October 2017

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

Structural highlights

2prq is a 1 chain structure with sequence from "aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1amp, 1lok
Activity:	Bacterial leucyl aminopeptidase, with EC number 3.4.11.10
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-helices, identical to [ZnZn(AAP)]. Co(II) binding to AAP does not introduce any major conformational changes to the overall protein structure and the amino acid residues ligated to the dicobalt(II) cluster in [CoCo(AAP)] are the same as those in the native Zn(II)-loaded structure with only minor perturbations in bond lengths. The Co(II)-Co(II) distance is 3.3A. Tris(hydroxymethyl)aminomethane (Tris) coordinates to the dinuclear Co(II) active site of AAP with one of the Tris hydroxyl oxygen atoms (O4) forming a single oxygen atom bridge between the two Co(II) ions. This is the only Tris atom coordinated to the metals with Co1-O and Co2-O bonds distances of 2.2 and 1.9A, respectively. Each of the Co(II) ions resides in a distorted trigonal bipyramidal geometry. This important structure bridges the gap between previous structural and spectroscopic studies performed on AAP and is discussed in this context.

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica.,Munih P, Moulin A, Stamper CC, Bennett B, Ringe D, Petsko GA, Holz RC J Inorg Biochem. 2007 Aug;101(8):1099-107. Epub 2007 Apr 11. PMID:17574677^[1]

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

References

↑ Munih P, Moulin A, Stamper CC, Bennett B, Ringe D, Petsko GA, Holz RC. X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica. J Inorg Biochem. 2007 Aug;101(8):1099-107. Epub 2007 Apr 11. PMID:17574677 doi:10.1016/j.jinorgbio.2007.03.010

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2prq"

@@ Line 1: / Line 1: @@
 ==X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica==
 <StructureSection load='2prq' size='340' side='right' caption='[[2prq]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1amp|1amp]], [[1lok|1lok]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </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=2prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prq OCA], [http://pdbe.org/2prq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2prq RCSB], [http://www.ebi.ac.uk/pdbsum/2prq 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=2prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prq OCA], [http://pdbe.org/2prq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2prq RCSB], [http://www.ebi.ac.uk/pdbsum/2prq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2prq ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 2prq" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Aminopeptidase|Aminopeptidase]]
 == References ==
 <references/>

2prq

From Proteopedia

Revision as of 09:31, 18 October 2017

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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