1m4l

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{{Seed}}
 
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[[Image:1m4l.png|left|200px]]
 
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==STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1m4l", creates the "Structure Box" on the page.
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<StructureSection load='1m4l' size='340' side='right'caption='[[1m4l]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m4l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1m4l| PDB=1m4l | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4l OCA], [https://pdbe.org/1m4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4l RCSB], [https://www.ebi.ac.uk/pdbsum/1m4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CBPA1_BOVIN 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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/1m4l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m4l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION===
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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<ref>PMID:12554943</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1m4l" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12554943}}, adds the Publication Abstract to the page
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12554943 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12554943}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1M4L is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4L OCA].
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==Reference==
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<ref group="xtra">PMID:12554943</ref><references group="xtra"/>
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Carboxypeptidase A]]
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[[Category: Large Structures]]
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[[Category: Glick, M.]]
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[[Category: Glick M]]
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[[Category: Goldblum, A.]]
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[[Category: Goldblum A]]
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[[Category: Greenblatt, H M.]]
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[[Category: Greenblatt HM]]
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[[Category: Kilshtain-Vardi, A.]]
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[[Category: Kilshtain-Vardi A]]
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[[Category: Shoham, G.]]
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[[Category: Shoham G]]
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[[Category: Carboxypeptidase some]]
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[[Category: Metalloexoproteinase]]
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[[Category: Metalloproteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:55:26 2009''
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Current revision

STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION

PDB ID 1m4l

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