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The | ==Crystal Structure of a Bacillus anthracis peptidoglycan deacetylase== | ||
<StructureSection load='6go1' size='340' side='right'caption='[[6go1]], [[Resolution|resolution]] 2.59Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6go1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GO1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yxkH, BA_0331, BASH2_05488 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 "Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</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=6go1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6go1 OCA], [http://pdbe.org/6go1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6go1 RCSB], [http://www.ebi.ac.uk/pdbsum/6go1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6go1 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ba0331 is a putative polysaccharide deacetylase from Bacillus anthracis, the etiological agent of the disease anthrax, that contributes to adaptation of the bacterium under extreme conditions and to maintenance of the cell shape. In the present study, the crystal structure of Ba0331 was determined at 2.6 A resolution. The structure consists of two domains: a fibronectin type 3-like (Fn3-like) domain and a NodB catalytic domain. The latter is present in all carbohydrate esterase family 4 enzymes, while a comparative analysis of the Fn3-like domain revealed structural plasticity despite the retention of the conserved Fn3-like domain characteristics. | |||
The putative polysaccharide deacetylase Ba0331: cloning, expression, crystallization and structure determination.,Andreou A, Giastas P, Arnaouteli S, Tzanodaskalaki M, Tzartos SJ, Bethanis K, Bouriotis V, Eliopoulos EE Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):312-320. doi:, 10.1107/S2053230X19001766. Epub 2019 Apr 3. PMID:30950833<ref>PMID:30950833</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6go1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Andreou, A]] | |||
[[Category: Eliopoulos, E E]] | |||
[[Category: Giastas, P]] | |||
[[Category: Bacillus anthracis]] | |||
[[Category: Deacetylase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Peptidoglycan]] | |||
Latest revision as of 09:50, 17 April 2019
Crystal Structure of a Bacillus anthracis peptidoglycan deacetylaseCrystal Structure of a Bacillus anthracis peptidoglycan deacetylase
Structural highlights
Publication Abstract from PubMedBa0331 is a putative polysaccharide deacetylase from Bacillus anthracis, the etiological agent of the disease anthrax, that contributes to adaptation of the bacterium under extreme conditions and to maintenance of the cell shape. In the present study, the crystal structure of Ba0331 was determined at 2.6 A resolution. The structure consists of two domains: a fibronectin type 3-like (Fn3-like) domain and a NodB catalytic domain. The latter is present in all carbohydrate esterase family 4 enzymes, while a comparative analysis of the Fn3-like domain revealed structural plasticity despite the retention of the conserved Fn3-like domain characteristics. The putative polysaccharide deacetylase Ba0331: cloning, expression, crystallization and structure determination.,Andreou A, Giastas P, Arnaouteli S, Tzanodaskalaki M, Tzartos SJ, Bethanis K, Bouriotis V, Eliopoulos EE Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):312-320. doi:, 10.1107/S2053230X19001766. Epub 2019 Apr 3. PMID:30950833[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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