This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3tf4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3tf4" [edit=sysop:move=sysop])
Current revision (11:33, 10 December 2016) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3tf4.png|left|200px]]
 
-
{{STRUCTURE_3tf4| PDB=3tf4 | SCENE= }}
+
==ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA==
 +
<StructureSection load='3tf4' size='340' side='right' caption='[[3tf4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3tf4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TF4 FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAMH1-PST1 FRAGMENT OF T. FUSC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2021 "Thermonospora fusca" Henssen 1957])</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tf4 OCA], [http://pdbe.org/3tf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tf4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tf4 ProSAT]</span></td></tr>
 +
</table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/3tf4_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3tf4 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA===
+
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<ref>PMID:9334746</ref>
-
{{ABSTRACT_PUBMED_9334746}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 3tf4" style="background-color:#fffaf0;"></div>
-
[[3tf4]] is a 2 chain structure of [[Glucanase]] with sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TF4 OCA].
+
==See Also==
==See Also==
*[[Glucanase|Glucanase]]
*[[Glucanase|Glucanase]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:009334746</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
 +
[[Category: Thermonospora fusca henssen 1957]]
[[Category: Cellulase]]
[[Category: Cellulase]]
-
[[Category: Thermobifida fusca]]
+
[[Category: Karplus, P A]]
-
[[Category: Karplus, P A.]]
+
[[Category: Sakon, J]]
-
[[Category: Sakon, J.]]
+
[[Category: Wilson, D B]]
-
[[Category: Wilson, D B.]]
+
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]

Current revision

ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA

3tf4, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools