1wkr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1wkr.gif|left|200px]]
[[Image:1wkr.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1wkr |SIZE=350|CAPTION= <scene name='initialview01'>1wkr</scene>, resolution 1.30&Aring;
+
The line below this paragraph, containing "STRUCTURE_1wkr", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=STA:STATINE'>STA</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Polyporopepsin Polyporopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.29 3.4.23.29] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1wkr| PDB=1wkr | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wkr OCA], [http://www.ebi.ac.uk/pdbsum/1wkr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wkr RCSB]</span>
+
-
}}
+
'''Crystal structure of aspartic proteinase from Irpex lacteus'''
'''Crystal structure of aspartic proteinase from Irpex lacteus'''
Line 31: Line 28:
[[Category: Kobayashi, H.]]
[[Category: Kobayashi, H.]]
[[Category: Mizuno, H.]]
[[Category: Mizuno, H.]]
-
[[Category: enzyme-inhibitor complex]]
+
[[Category: Enzyme-inhibitor complex]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:48:58 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:37:31 2008''
+

Revision as of 10:48, 3 May 2008

Template:STRUCTURE 1wkr

Crystal structure of aspartic proteinase from Irpex lacteus


Overview

The crystal structure of Irpex lacteus aspartic proteinase (ILAP) in complex with pepstatin (a six amino acid residue peptide-like inhibitor) was determined at 1.3A resolution. ILAP is a pepsin-like enzyme, widely distributed in nature, with high milk-clotting activity relative to proteolytic activity. The overall structure was in good topological agreement with pepsin and other aspartic proteases. The structure and interaction pattern around the catalytic site were conserved, in agreement with the other aspartic proteinase/inhibitor complex structures reported previously. The high-resolution data also supported the transition state model, as proposed previously for the catalytic mechanism of aspartic proteinase. Unlike the other aspartic proteinases, ILAP was found to require hydrophobic residues either in the P(1) or P(1') site, and also in the P(4) and/or P(3) site(s) for secondary interactions. The inhibitor complex structure also revealed the substrate binding mechanism of ILAP at the P(3) and P(4) site of the substrate, where the inserted loop built up the unique hydrophobic pocket at the P(4) site.

About this Structure

1WKR is a Single protein structure of sequence from Irpex lacteus. Full crystallographic information is available from OCA.

Reference

Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin., Fujimoto Z, Fujii Y, Kaneko S, Kobayashi H, Mizuno H, J Mol Biol. 2004 Aug 27;341(5):1227-35. PMID:15321718 Page seeded by OCA on Sat May 3 13:48:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools