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2ctc

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Revision as of 07:05, 29 November 2017

THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND L-PHENYL LACTATE

Structural highlights

2ctc is a 1 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Carboxypeptidase A, with EC number 3.4.17.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CBPA1_BOVIN] Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (By similarity).

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 structures of native carboxypeptidase A and of the enzyme-inhibitor complex with L-phenyl lactate have been refined at 1.54 and 1.45 A resolution to R factors of 0.151 and 0.161, respectively. Crystals of the complex were isomorphous with the native crystals (space group P2(1), a = 51.60, b = 60.27, c = 47.25 A, beta = 97.27 degrees ). The high-resolution electron density allowed correction of many side-chain positions in the classical carboxypeptidase A model. This reflects the advantages of the high-quality complete synchrotron data collected with an imaging plate detector. The conformational changes in the active centre of the enzyme upon binding of the inhibitor are restricted to only two residues, Tyr248 and Arg145. L-Phenyl lactate is bound in the S1' pocket and forms hydrogen bonds to Arg145, Glu270 and to the zinc-bound water molecule. The present structure provides an explanation for the higher stability of the complexes with the products of esterolysis in comparison with those of amidolysis. This is consistent with the finding that product release is rate limiting for esters but not for peptides.

High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate.,Teplyakov A, Wilson KS, Orioli P, Mangani S Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):534-40. PMID:15299490^[1]

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

References

↑ Teplyakov A, Wilson KS, Orioli P, Mangani S. High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate. Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):534-40. PMID:15299490 doi:http://dx.doi.org/10.1107/S0907444993007267

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/2ctc"

@@ Line 1: / Line 1: @@
 ==THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND L-PHENYL LACTATE==
 <StructureSection load='2ctc' size='340' side='right' caption='[[2ctc]], [[Resolution|resolution]] 1.40&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=HFA:ALPHA-HYDROXY-BETA-PHENYL-PROPIONIC+ACID'>HFA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1] </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=2ctc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ctc OCA], [http://pdbe.org/2ctc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ctc RCSB], [http://www.ebi.ac.uk/pdbsum/2ctc 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=2ctc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ctc OCA], [http://pdbe.org/2ctc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ctc RCSB], [http://www.ebi.ac.uk/pdbsum/2ctc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ctc ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2ctc" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Carboxypeptidase|Carboxypeptidase]]
 == References ==
 <references/>

2ctc

From Proteopedia

Revision as of 07:05, 29 November 2017

THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND L-PHENYL LACTATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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