1qqu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qqu.gif|left|200px]]<br /><applet load="1qqu" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1qqu.gif|left|200px]]
-
caption="1qqu, resolution 1.63&Aring;" />
+
 
-
'''CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH BOUND ACETATE ION'''<br />
+
{{Structure
 +
|PDB= 1qqu |SIZE=350|CAPTION= <scene name='initialview01'>1qqu</scene>, resolution 1.63&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4]
 +
|GENE=
 +
}}
 +
 
 +
'''CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH BOUND ACETATE ION'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1QQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQU OCA].
+
1QQU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQU OCA].
==Reference==
==Reference==
-
Crystal structure at 1.63 A resolution of the native form of porcine beta-trypsin: revealing an acetate ion binding site and functional water network., Johnson A, Gautham N, Pattabhi V, Biochim Biophys Acta. 1999 Nov 16;1435(1-2):7-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10561533 10561533]
+
Crystal structure at 1.63 A resolution of the native form of porcine beta-trypsin: revealing an acetate ion binding site and functional water network., Johnson A, Gautham N, Pattabhi V, Biochim Biophys Acta. 1999 Nov 16;1435(1-2):7-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10561533 10561533]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
Line 22: Line 31:
[[Category: serine protease]]
[[Category: serine protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:44 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:41:28 2008''

Revision as of 11:41, 20 March 2008

Image:1qqu.gif


PDB ID 1qqu

Drag the structure with the mouse to rotate
, resolution 1.63Å
Ligands: and
Activity: Trypsin, with EC number 3.4.21.4
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH BOUND ACETATE ION


Overview

The active center of a serine protease is the catalytic triad composed of His-57, Ser-195 and Asp-102. The existing crystal structure data on serine proteases have not fully answered a number of fundamental questions relating to the catalytic activity of serine proteases. The new high resolution native porcine beta-trypsin (BPT) structure is aimed at extending the knowledge on the conformation of the active site and the ordered water structure within and around the active site. The crystal structure of BPT has been determined at 1.63 A resolution. An acetate ion bound at the active site of a trypsin molecule by both classical hydrogen bonds and C-HellipsisO hydrogen bonds has been identified for the first time. A large network of water molecules extending from the recognition amino acid Asp-184 to the entry of the active site has been observed in the BPT structure. A detailed comparison with inhibitor complexes and autolysates indicates that the sulfate ion and the acetate ion bind at the same site of the trypsin molecule. The Ser-195 Cbeta-Ogamma-His-57 Nepsilon angle in the catalytic triad of BPT is intermediate between the corresponding values of the complex and native structure due to acetate ion binding. The network of waters from the recognition amino acid to the active site entry is probably the first ever complete picture of functional waters around the active site. Structural comparisons show that the functional waters involved in the binding of small molecule inhibitors and protease inhibitors are distinctly different.

About this Structure

1QQU is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystal structure at 1.63 A resolution of the native form of porcine beta-trypsin: revealing an acetate ion binding site and functional water network., Johnson A, Gautham N, Pattabhi V, Biochim Biophys Acta. 1999 Nov 16;1435(1-2):7-21. PMID:10561533

Page seeded by OCA on Thu Mar 20 13:41:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qqu"
Personal tools