1pyt

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[[Image:1pyt.gif|left|200px]]
[[Image:1pyt.gif|left|200px]]
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{{Structure
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|PDB= 1pyt |SIZE=350|CAPTION= <scene name='initialview01'>1pyt</scene>, resolution 2.35&Aring;
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The line below this paragraph, containing "STRUCTURE_1pyt", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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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{{STRUCTURE_1pyt| PDB=1pyt | 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=1pyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pyt OCA], [http://www.ebi.ac.uk/pdbsum/1pyt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pyt RCSB]</span>
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'''TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C'''
'''TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C'''
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[[Category: Gomis-Ruth, F X.]]
[[Category: Gomis-Ruth, F X.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
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[[Category: c-terminal peptidase]]
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[[Category: C-terminal peptidase]]
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[[Category: serine proteinase]]
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[[Category: Serine proteinase]]
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[[Category: ternary complex (zymogen)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:39:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:24 2008''
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Revision as of 02:39, 3 May 2008

Template:STRUCTURE 1pyt

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


Overview

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.

About this Structure

1PYT is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

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:7556081 Page seeded by OCA on Sat May 3 05:39:20 2008

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