1cpx: Difference between revisions

Revision as of 21:04, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1cpx.png

Template:STRUCTURE 1cpx

BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.

Template:ABSTRACT PUBMED 9843422

About this StructureAbout this Structure

1CPX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248., Bukrinsky JT, Bjerrum MJ, Kadziola A, Biochemistry. 1998 Nov 24;37(47):16555-64. PMID:9843422

Page seeded by OCA on Mon Jun 30 21:04:45 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1cpx.jpg|left|200px]]
+{{Seed}}
+[[Image:1cpx.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1cpx|  PDB=1cpx  |  SCENE=  }}
-'''BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.'''
+===BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.===
-==Overview==
+<!--
-Native carboxypeptidase A has been crystallized in a new crystal form, and the structure has been refined with X-ray data to 2.0 A resolution. In contrast to the previously published structure [Rees, D. C., Lewis, M., and Lipscomb, W. N. (1983) J. Mol. Biol. 168, 367-387], no active-site amino acids are involved in the crystal packing. The important Tyr248 is stabilized inside the active site by a hydrogen bond and by interactions with Ile247. The proposed role of Tyr248 in the induced fit mechanism is therefore not supported by the findings in this structure of native carboxypeptidase A. The structure has a partly populated inhibitory Zn2+ site in close proximity to the catalytic Zn2+ as evident from X-ray anomalous dispersion data. A hydroxo bridge is found between the catalytic Zn2+ and the inhibitory Zn2+ with a Zn2+-Zn2+ distance of 3.48 A. In addition, the inhibitory Zn2+ has Glu270 as a monodentate ligand. No other protein ligands to the inhibitory Zn2+ are seen. The crystals were grown at 0.3 M LiCl and weak evidence for a binding site for partly competitive inhibitory anions is observed.
+The line below this paragraph, {{ABSTRACT_PUBMED_9843422}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9843422 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9843422}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Metalloprotease]]
 [[Category: Zinc inhibition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:59:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:04:45 2008''