1m4l

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[[Image:1m4l.gif|left|200px]]
[[Image:1m4l.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1m4l |SIZE=350|CAPTION= <scene name='initialview01'>1m4l</scene>, resolution 1.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1m4l", 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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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1m4l| PDB=1m4l | SCENE= }}
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|RELATEDENTRY=[[1yme|1YME]], [[2ctb|2CTB]], [[5cpa|5CPA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4l OCA], [http://www.ebi.ac.uk/pdbsum/1m4l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m4l RCSB]</span>
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}}
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'''STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION'''
'''STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION'''
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[[Category: Metalloexoproteinase]]
[[Category: Metalloexoproteinase]]
[[Category: Metalloproteinase]]
[[Category: Metalloproteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:37:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Apr 5 19:17:27 2008''
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Revision as of 21:37, 2 May 2008

Image:1m4l.gif

Template:STRUCTURE 1m4l

STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION


Overview

The crystal structure of the bovine zinc metalloproteinase carboxypeptidase A (CPA) has been refined to 1.25 A resolution based on room-temperature X-ray synchrotron data. The significantly improved structure of CPA at this resolution (anisotropic temperature factors, R factor = 10.4%, R(free) = 14.5%) allowed the modelling of conformational disorders of side chains, improved the description of the protein solvent network (375 water molecules) and provided a more accurate picture of the interactions between the active-site zinc and its ligands. The calculation of standard uncertainties in individual atom positions of the refined model of CPA allowed the deduction of the protonation state of some key residues in the active site and confirmed that Glu72 and Glu270 are negatively charged in the resting state of the enzyme at pH 7.5. These results were further validated by theoretical calculations that showed significant reduction of the pK(a) of these side chains relative to solution values. The distance between the zinc-bound solvent molecule and the metal ion is strongly suggestive of a neutral water molecule and not a hydroxide ion in the resting state of the enzyme. These findings could support both the general acid/general base mechanism, as well as the anhydride mechanism suggested for CPA.

About this Structure

1M4L is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Refined structure of bovine carboxypeptidase A at 1.25 A resolution., Kilshtain-Vardi A, Glick M, Greenblatt HM, Goldblum A, Shoham G, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):323-33. Epub 2003, Jan 23. PMID:12554943 Page seeded by OCA on Sat May 3 00:37:19 2008

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