1rd6: Difference between revisions

New page: left|200px<br /><applet load="1rd6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rd6, resolution 2.60Å" /> '''Crystal Structure of...
 
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[[Image:1rd6.gif|left|200px]]<br /><applet load="1rd6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rd6, resolution 2.60&Aring;" />
'''Crystal Structure of S. Marcescens Chitinase A Mutant W167A'''<br />


==About this Structure==
==Crystal Structure of S. Marcescens Chitinase A Mutant W167A==
1RD6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RD6 OCA].  
<StructureSection load='1rd6' size='340' side='right'caption='[[1rd6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
[[Category: Chitinase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[1rd6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RD6 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]] 2.6&#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=1rd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rd6 OCA], [https://pdbe.org/1rd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rd6 RCSB], [https://www.ebi.ac.uk/pdbsum/1rd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rd6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHIA_SERMA CHIA_SERMA]
== 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/rd/1rd6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1rd6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Family 18 chitinases have the signature peptide DGXDXDXE forming the fourth beta-strand in the (beta/alpha)8-barrel of their catalytic domain. The carboxyl-end glutamic acid, E315 in Serratia marcescens chitinase A, serves as the acid/base during chitin hydrolysis, and the side-chain of the preceding aspartic acid, D313, helps to position correctly the N-acetyl moiety of the glycosyl sugar undergoing hydrolysis. Chitin substrates are bound within a long cleft across the top of the barrel, whose floor consists of aromatic residues that hydrophobically stack with every other GlcNAc. Alanine substitution of the conserved Trp167 at the -3 subsite in Serratia marcescens chitinase A enhanced transglycosylation. Higher oligosaccharides were formed from both chitin tetra- and pentasaccharide, and the only hydrolytic product from chitin trisaccharide was the disaccharide. Greater retention of the glycosyl fragment at the active site of the -3 mutant of Serratia marcescens chitinase A might favor transglycosylation due to a stabilized conformation of its D313.
 
Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.,Aronson NN Jr, Halloran BA, Alexeyev MF, Zhou XE, Wang Y, Meehan EJ, Chen L Biosci Biotechnol Biochem. 2006 Jan;70(1):243-51. PMID:16428843<ref>PMID:16428843</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1rd6" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Chitinase 3D structures|Chitinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
[[Category: Single protein]]
[[Category: Alexyev MF]]
[[Category: Alexyev, M.F.]]
[[Category: Aronson NN]]
[[Category: Chen, L.]]
[[Category: Chen L]]
[[Category: Halloran, B.A.]]
[[Category: Halloran BA]]
[[Category: JR., N.N.Aronson.]]
[[Category: Meehan EJ]]
[[Category: Meehan, E.J.]]
[[Category: Wang Y]]
[[Category: Wang, Y.]]
[[Category: Zhou XE]]
[[Category: Zhou, X.E.]]
[[Category: chitinase a]]
 
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