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4l1g

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Current revision

Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus

Structural highlights

4l1g is a 4 chain structure with sequence from Bacillus cereus ATCC 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.336Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Psylinakis E, Boneca IG, Mavromatis K, Deli A, Hayhurst E, Foster SJ, Vårum KM, Bouriotis V. Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis. J Biol Chem. 2005 Sep 2;280(35):30856-63. PMID:15961396 doi:10.1074/jbc.M407426200
↑ Balomenou S, Koutsioulis D, Tomatsidou A, Tzanodaskalaki M, Petratos K, Bouriotis V. Polysaccharide deacetylases serve as new targets for the design of inhibitors against Bacillus anthracis and Bacillus cereus. Bioorg Med Chem. 2018 Jul 30;26(13):3845-3851. PMID:29983281 doi:10.1016/j.bmc.2018.06.045
↑ 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. An unusual alpha-carbon hydroxylation of proline promotes active-site maturation. J Am Chem Soc. 2017 Mar 23. doi: 10.1021/jacs.6b12209. PMID:28333455 doi:http://dx.doi.org/10.1021/jacs.6b12209

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4l1g"

Categories: Bacillus cereus ATCC 14579 | Large Structures | Fadouloglou VE | Kokkinidis M | Tsalafouta A

@@ Line 3: / Line 3: @@
 <StructureSection load='4l1g' size='340' side='right'caption='[[4l1g]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4l1g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. 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 [http://oca.weizmann.ac.il/oca-docs/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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.336&#8491;</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=PXU:2-HYDROXY-L-PROLINE'>PXU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bc1960, BC_1960 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</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>
-<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=4l1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1g OCA], [http://pdbe.org/4l1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l1g RCSB], [http://www.ebi.ac.uk/pdbsum/4l1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1g ProSAT]</span></td></tr>
 </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 ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Baccr]]
+[[Category: Bacillus cereus ATCC 14579]]
 [[Category: Large Structures]]
-[[Category: Fadouloglou, V E]]
+[[Category: Fadouloglou VE]]
-[[Category: Kokkinidis, M]]
+[[Category: Kokkinidis M]]
-[[Category: Tsalafouta, A]]
+[[Category: Tsalafouta A]]
-[[Category: Hydrolase]]
-[[Category: Polysaccharide deacetylase]]
-[[Category: Tim barrel]]

4l1g

From Proteopedia

Current revision

Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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