1yme

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[[Image:1yme.jpg|left|200px]]
[[Image:1yme.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1yme |SIZE=350|CAPTION= <scene name='initialview01'>1yme</scene>, resolution 1.53&Aring;
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The line below this paragraph, containing "STRUCTURE_1yme", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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|GENE=
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{{STRUCTURE_1yme| PDB=1yme | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yme OCA], [http://www.ebi.ac.uk/pdbsum/1yme PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yme RCSB]</span>
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'''STRUCTURE OF CARBOXYPEPTIDASE'''
'''STRUCTURE OF CARBOXYPEPTIDASE'''
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[[Category: Shoham, G.]]
[[Category: Shoham, G.]]
[[Category: Tucker, P A.]]
[[Category: Tucker, P A.]]
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[[Category: carboxypeptidase]]
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[[Category: Carboxypeptidase]]
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[[Category: metalloexoproteinase]]
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[[Category: Metalloexoproteinase]]
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[[Category: metalloproteinase]]
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[[Category: Metalloproteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:30:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:13:05 2008''
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Revision as of 13:30, 3 May 2008

Image:1yme.jpg

Template:STRUCTURE 1yme

STRUCTURE OF CARBOXYPEPTIDASE


Overview

The crystal structure of the zinc-containing exopeptidase bovine carboxypeptidase A (CPA) has been refined to high resolution, based on a data set collected from a single crystal, incorporating new sequence information based on cloning of the bovine gene. In addition, new refined structures are available for the zinc-removed form of the enzyme, apo-CPA, as well as the mercury-replaced form, Hg-CPA. The native structure reveals that the zinc-bound water molecule does not appear to more loosely bound than the rest of the zinc ligands, at least when B-factor values are considered. Nor is there any evidence for a secondary location of this water molecule. The apo-enzyme structure does not show any density in the place of the removed zinc ion. The only significant change appears to be a chi2 rotation of one zinc histidine ligand to form an ion-pair interaction with a glutamic acid side chain. The structure of Hg-CPA reveals a solvent Tris molecule bound to the mercury cation, as well as an unidentified cation bound to Glu270. The location of this citation agrees with previous proposals for the binding side of inhibitory zinc. These observations may explain some of the differences in kinetics observed in metal- replaced CPA.

About this Structure

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

Reference

Carboxypeptidase A: native, zinc-removed and mercury-replaced forms., Greenblatt HM, Feinberg H, Tucker PA, Shoham G, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):289-305. PMID:9867434 Page seeded by OCA on Sat May 3 16:30:35 2008

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