3tf4: Difference between revisions

Revision as of 13:08, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3tf4.png

Template:STRUCTURE 3tf4

ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORAENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA

Template:ABSTRACT PUBMED 9334746

About this StructureAbout this Structure

3TF4 is a Single protein structure of sequence from Thermobifida fusca. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca., Sakon J, Irwin D, Wilson DB, Karplus PA, Nat Struct Biol. 1997 Oct;4(10):810-8. PMID:9334746

Page seeded by OCA on Thu Jul 3 13:08:34 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:3tf4.jpg|left|200px]]
+{{Seed}}
+[[Image:3tf4.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3tf4|  PDB=3tf4  |  SCENE=  }}
-'''ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA'''
+===ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA===
-==Overview==
+<!--
-Cellulase E4 from Thermomonospora fusca is unusual in that it has characteristics of both exo- and endo-cellulases. Here we report the crystal structure of a 68K M(r) fragment of E4 (E4-68) at 1.9 A resolution. E4-68 contains both a family 9 catalytic domain, exhibiting an (alpha/alpha)6 barrel fold, and a family III cellulose binding domain, having an antiparallel beta-sandwich fold. While neither of these folds is novel, E4-68 provides the first cellulase structure having interacting catalytic and cellulose binding domains. The complexes of E4-68 with cellopentaose, cellotriose and cellobiose reveal conformational changes associated with ligand binding and allow us to propose a catalytic mechanism for family 9 enzymes. We also provide evidence that E4 has two novel characteristics: first it combines exo- and endo-activities and second, when it functions as an exo-cellulase, it cleaves off cellotetraose units.
+The line below this paragraph, {{ABSTRACT_PUBMED_9334746}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9334746 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9334746}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Wilson, D B.]]
 [[Category: Glycosyl hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:13:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:08:34 2008''