View source for 4atw


==The crystal structure of Arabinofuranosidase==
<StructureSection load='4atw' size='340' side='right'caption='[[4atw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4atw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ATW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4atw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atw OCA], [https://pdbe.org/4atw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4atw RCSB], [https://www.ebi.ac.uk/pdbsum/4atw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4atw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9WYB7_THEMA Q9WYB7_THEMA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An alpha-L-arabinofuranosidase (TmAFase) from Thermotoga maritima MSB8 is a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes. In the present study, we carried out the enzymatic characterization and structural analysis of TmAFase. Tight domain associations found in TmAFase, such as an inter-domain disulfide bond (Cys306 and Cys476) in each monomer, a novel extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) was identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates.

Structural Analysis of alpha-L-Arabinofuranosidase from Thermotoga maritima Reveals Characteristics for Thermostability and Substrate Specificity.,Dumbrepatil A, Park JM, Jung TY, Song HN, Jang MU, Han NS, Kim TJ, Woo EJ J Microbiol Biotechnol. 2012 Dec;22(12):1724-30. PMID:23221536<ref>PMID:23221536</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4atw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Dumbrepatil A]]
[[Category: Jung T-Y]]
[[Category: Kim T-J]]
[[Category: Song H-N]]
[[Category: Woo E-J]]