4l1g
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus== | ==Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus== | ||
| - | <StructureSection load='4l1g' size='340' side='right'caption='[[4l1g]]' scene=''> | + | <StructureSection load='4l1g' size='340' side='right'caption='[[4l1g]], [[Resolution|resolution]] 2.34Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L1G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l1g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L1G FirstGlance]. <br> |
| - | </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=4l1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1g OCA], [https://pdbe.org/4l1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l1g RCSB], [https://www.ebi.ac.uk/pdbsum/4l1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1g ProSAT]</span></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]] 2.336Å</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=PXU:2-HYDROXY-L-PROLINE'>PXU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4l1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1g OCA], [https://pdbe.org/4l1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l1g RCSB], [https://www.ebi.ac.uk/pdbsum/4l1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PGDA1_BACCR PGDA1_BACCR] Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PubMed:15961396, PubMed:29983281). Also acts on soluble chitin substrates and N-acetylchitooligomers. Acts on cell wall peptidoglycan from the Gram-positive bacteria B.cereus and B.subtilis and the Gram-negative bacterium H.pylori. Not active on acetylated xylan (PubMed:15961396).<ref>PMID:15961396</ref> <ref>PMID:29983281</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The full extent of proline (Pro) hydroxylation has yet to be established, as it is largely unexplored in bacteria. We describe here a so far unknown Pro hydroxylation activity which occurs in active sites of polysaccharide deacetylases (PDAs) from bacterial pathogens, modifying the protein backbone at the Calpha atom of a Pro residue to produce 2-hydroxyproline (2-Hyp). This process modifies with high specificity a conserved Pro, shares with the deacetylation reaction the same active site and one cata-lytic residue and utilizes molecular oxygen as source for the hydroxyl group oxygen of 2-Hyp. By providing additional hydrogen bonding capacity, the Pro-->2-Hyp conversion alters the active site and enhances significantly deacetylase activity, probably by creating a more favorable environment for transition state stabilization. Our results classify this process as an active site "maturation", which is highly atypical by being a protein backbone modifying activity, rather than a side-chain modifying one. | ||
| + | |||
| + | An unusual alpha-carbon hydroxylation of proline promotes active-site maturation.,Fadouloglou VE, Balomenou S, Aivaliotis M, Kotsifaki D, Arnaouteli S, Tomatsidou A, Efstathiou G, Kountourakis N, Miliara S, Griniezaki M, Tsalafouta A, Pergantis SA, Boneca IG, Glykos NM, Bouriotis V, Kokkinidis M J Am Chem Soc. 2017 Mar 23. doi: 10.1021/jacs.6b12209. PMID:28333455<ref>PMID:28333455</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4l1g" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus cereus ATCC 14579]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fadouloglou VE]] | [[Category: Fadouloglou VE]] | ||
[[Category: Kokkinidis M]] | [[Category: Kokkinidis M]] | ||
[[Category: Tsalafouta A]] | [[Category: Tsalafouta A]] | ||
Current revision
Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus
| |||||||||||
