We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1wqs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
Norovirus 3C-like proteases are crucial to proteolytic processing of, norovirus polyproteins. We determined the crystal structure of the 3C-like, protease from Chiba virus, a norovirus, at 2.8-A resolution. An active, site including Cys139 and His30 is present, as is a hydrogen bond network, that stabilizes the active site conformation. In the oxyanion hole, backbone, a structural difference was observed probably upon substrate, binding. A peptide substrate/enzyme model shows that several interactions, between the two components are critical for substrate binding and that the, S1 and S2 sites appropriately accommodate the substrate P1 and P2, residues, respectively. Knowledge of the structure and a previous, mutagenesis study allow us to correlate proteolysis and structure.
+
Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.
==About this Structure==
==About this Structure==
Line 27: Line 27:
[[Category: oxyanion hole]]
[[Category: oxyanion hole]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:42:05 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:11 2008''

Revision as of 13:47, 21 February 2008


1wqs, resolution 2.80Å

Drag the structure with the mouse to rotate

Crystal structure of Norovirus 3C-like protease

Overview

Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.

About this Structure

1WQS is a Single protein structure of sequence from Chiba virus with , and as ligands. Full crystallographic information is available from OCA.

Reference

A norovirus protease structure provides insights into active and substrate binding site integrity., Nakamura K, Someya Y, Kumasaka T, Ueno G, Yamamoto M, Sato T, Takeda N, Miyamura T, Tanaka N, J Virol. 2005 Nov;79(21):13685-93. PMID:16227288

Page seeded by OCA on Thu Feb 21 15:47:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools