1pyt: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1pyt.gif|left|200px]]<br /><applet load="1pyt" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1pyt.gif|left|200px]]
caption="1pyt, resolution 2.35&Aring;" />
 
'''TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C'''<br />
{{Structure
|PDB= 1pyt |SIZE=350|CAPTION= <scene name='initialview01'>1pyt</scene>, resolution 2.35&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''TERNARY COMPLEX OF PROCARBOXYPEPTIDASE A, PROPROTEINASE E, AND CHYMOTRYPSINOGEN C'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
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 <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ZN:'>ZN</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYT OCA].  
1PYT is a [[Protein complex]] structure of sequences 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=1PYT OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7556081 7556081]
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://www.ncbi.nlm.nih.gov/pubmed/7556081 7556081]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Carboxypeptidase A]]
[[Category: Carboxypeptidase A]]
Line 25: Line 34:
[[Category: ternary complex (zymogen)]]
[[Category: ternary complex (zymogen)]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:59 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:30:45 2008''

Revision as of 14:30, 20 March 2008

File:1pyt.gif


PDB ID 1pyt

Drag the structure with the mouse to rotate
, resolution 2.35Å
Ligands: and
Activity: Carboxypeptidase A, with EC number 3.4.17.1
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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 Thu Mar 20 13:30:45 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA