1pyt: Difference between revisions

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New page: left|200px<br /><applet load="1pyt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pyt, resolution 2.35Å" /> '''TERNARY COMPLEX OF P...
 
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[[Image:1pyt.gif|left|200px]]<br /><applet load="1pyt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1pyt, resolution 2.35&Aring;" />
'''TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C'''<br />


==Overview==
==TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C==
The metalloexozymogen procarboxypeptidase A is mainly secreted in, ruminants as a ternary complex with zymogens of two serine, endoproteinases, chymotrypsinogen C and proproteinase E. The bovine, complex has been crystallized, and its molecular structure analysed and, refined at 2.6 A resolution to an R factor of 0.198. In this heterotrimer, the activation segment of procarboxypeptidase A essentially clamps the, other two subunits, which shield the activation sites of the former from, tryptic attack. In contrast, the propeptides of both serine proproteinases, are freely accessible to trypsin. This arrangement explains the sequential, and delayed activation of the constituent zymogens. Procarboxypeptidase A, is virtually identical to the homologous monomeric porcine form., Chymotrypsinogen C displays structural features characteristic for, chymotrypsins as well as elastases, except for its activation domain;, similar to bovine chymotrypsinogen A, its binding site is not properly, formed, while its surface located activation segment is disordered. The, proproteinase E structure is fully ordered and strikingly similar to, active porcine elastase; its specificity pocket is occluded, while the, activation segment is fixed to the molecular surface. This first structure, of a native zymogen from the proteinase E/elastase family does not, fundamentally differ from the serine proproteinases known so far.
<StructureSection load='1pyt' size='340' side='right'caption='[[1pyt]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pyt]] is a 4 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=1PYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PYT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pyt OCA], [https://pdbe.org/1pyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pyt RCSB], [https://www.ebi.ac.uk/pdbsum/1pyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pyt ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/1pyt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1pyt ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1PYT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PYT OCA].
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
 
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
==Reference==
__TOC__
The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C., Gomis-Ruth FX, Gomez M, Bode W, Huber R, Aviles FX, EMBO J. 1995 Sep 15;14(18):4387-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7556081 7556081]
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Carboxypeptidase A]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Aviles FX]]
[[Category: Aviles, F.X.]]
[[Category: Bode W]]
[[Category: Bode, W.]]
[[Category: Gomez M]]
[[Category: Gomez, M.]]
[[Category: Gomis-Ruth FX]]
[[Category: Gomis-Ruth, F.X.]]
[[Category: Huber R]]
[[Category: Huber, R.]]
[[Category: CA]]
[[Category: ZN]]
[[Category: c-terminal peptidase]]
[[Category: serine proteinase]]
[[Category: ternary complex (zymogen)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:14:29 2007''

Latest revision as of 09:00, 17 April 2024

TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN CTERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C

Structural highlights

1pyt is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.35Å
Ligands:,
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.

See Also

1pyt, resolution 2.35Å

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