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| | <StructureSection load='4v33' size='340' side='right'caption='[[4v33]], [[Resolution|resolution]] 1.48Å' scene=''> | | <StructureSection load='4v33' size='340' side='right'caption='[[4v33]], [[Resolution|resolution]] 1.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v33]] 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=4V33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V33 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v33]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V33 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=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PXU:2-HYDROXY-L-PROLINE'>PXU</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PXU:2-HYDROXY-L-PROLINE'>PXU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4v33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v33 OCA], [http://pdbe.org/4v33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v33 RCSB], [http://www.ebi.ac.uk/pdbsum/4v33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v33 ProSAT]</span></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=4v33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v33 OCA], [https://pdbe.org/4v33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v33 RCSB], [https://www.ebi.ac.uk/pdbsum/4v33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v33 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A6L8P8I1_BACAN A0A6L8P8I1_BACAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bacillus anthracis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andreou, A]] | + | [[Category: Andreou A]] |
| - | [[Category: Bouriotis, V]] | + | [[Category: Bouriotis V]] |
| - | [[Category: Eliopoulos, E]] | + | [[Category: Eliopoulos E]] |
| - | [[Category: Giastas, P]] | + | [[Category: Giastas P]] |
| - | [[Category: Fibronectin type iii domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A0A6L8P8I1_BACAN
Publication Abstract from PubMed
Membrane-anchored lipoproteins have a broad range of functions and play key roles in several cellular processes in Gram-positive bacteria. BA0330 and BA0331 are the only lipoproteins among the 11 known or putative polysaccharide deacetylases of Bacillus anthacis. We found that both lipoproteins exhibit unique characteristics. BA0330 and BA0331 interact with peptidoglycan and BA0330 is important for the adaptation of the bacterium to grow in the presence of high concentration of salt, while BA0331 contributes to maintenance of a uniform cell shape. They appear not to alter the peptidoglycan structure and do not contribute to lysozyme resistance. The high-resolution X-ray structure of BA0330 revealed a C-terminal domain with the typical fold of a carbohydrate esterase 4, and an N-terminal domain unique for this family, composed of a two-layered (4 + 3) beta-sandwich with high similarity to Fibronectin type 3 domains. Our data suggest that BA0330 and BA0331 have a structural role in stabilizing the cell wall of B. anthracis.
Two putative polysaccharide deacetylases are required for osmotic stability and cell shape maintenance in Bacillus anthracis.,Arnaouteli S, Giastas P, Andreou A, Tzanodaskalaki M, Aldridge C, Tzartos SJ, Vollmer W, Eliopoulos E, Bouriotis V J Biol Chem. 2015 Mar 30. pii: jbc.M115.640029. PMID:25825488[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arnaouteli S, Giastas P, Andreou A, Tzanodaskalaki M, Aldridge C, Tzartos SJ, Vollmer W, Eliopoulos E, Bouriotis V. Two putative polysaccharide deacetylases are required for osmotic stability and cell shape maintenance in Bacillus anthracis. J Biol Chem. 2015 Mar 30. pii: jbc.M115.640029. PMID:25825488 doi:http://dx.doi.org/10.1074/jbc.M115.640029
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