5xw3: Difference between revisions
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<StructureSection load='5xw3' size='340' side='right' caption='[[5xw3]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='5xw3' size='340' side='right' caption='[[5xw3]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5xw3]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ql4 4ql4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XW3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5xw3]] 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]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ql4 4ql4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XW3 FirstGlance]. <br> | ||
</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=5xw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw3 OCA], [http://pdbe.org/5xw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xw3 RCSB], [http://www.ebi.ac.uk/pdbsum/5xw3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw3 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysM, GBAA_4601 ([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=5xw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw3 OCA], [http://pdbe.org/5xw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xw3 RCSB], [http://www.ebi.ac.uk/pdbsum/5xw3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The reverse transsulfuration pathway has been reported to produce cysteine from homocysteine in eukaryotes ranging from protozoans to mammals while bacteria and plants produce cysteine via a de novo pathway. Interestingly, the bacterium Bacillus anthracis includes enzymes of the reverse transsulfuration pathway viz. cystathionine beta-synthase [BaCBS, previously annotated to be an O-acetylserine sulfhydrylase (OASS)] and cystathionine gamma-lyase. Here, we report the structure of BaCBS at a resolution of 2.2 A. The enzyme was found to show CBS activity only with activated serine (O-acetylserine) and not with serine, and was also observed to display OASS activity but not serine sulfhydrylase activity. BaCBS was also found to produce hydrogen sulfide (H2 S) upon reaction of cysteine and homocysteine. A mutational study revealed Glu 220, conserved in CBS, to be necessary for generating H2 S. Structurally, BaCBS display a considerably more open active site than has been found for any other CBS or OASS, which was attributed to the presence of a helix at the junction of the C- and N-terminal domains. The root-mean-square deviation (RMSD) between the backbone Calpha carbon atoms of BaCBS and those of other CBSs and OASSs were calculated to be greater than 3.0 A. The pyridoxal 5'-phosphate at the active site was not traced, and appeared to be highly flexible due to the active site being wide open. Phylogenetic analysis revealed the presence of an O-acetylserine-dependent CBS in the bacterial domain and making separate clade from CBS and OASS indicating its evolution for specific function. DATABASE: Structural data are available in the PDB under the accession number 5XW3. | |||
Structural characterization and functional analysis of cystathionine beta-synthase: an enzyme involved in the reverse transsulfuration pathway of Bacillus anthracis.,Devi S, Abdul Rehman SA, Tarique KF, Gourinath S FEBS J. 2017 Sep 16. doi: 10.1111/febs.14273. PMID:28921884<ref>PMID:28921884</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5xw3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:17, 15 November 2017
Crystal structure of cystathionine beta-synthase from Bacillus anthracisCrystal structure of cystathionine beta-synthase from Bacillus anthracis
Structural highlights
Publication Abstract from PubMedThe reverse transsulfuration pathway has been reported to produce cysteine from homocysteine in eukaryotes ranging from protozoans to mammals while bacteria and plants produce cysteine via a de novo pathway. Interestingly, the bacterium Bacillus anthracis includes enzymes of the reverse transsulfuration pathway viz. cystathionine beta-synthase [BaCBS, previously annotated to be an O-acetylserine sulfhydrylase (OASS)] and cystathionine gamma-lyase. Here, we report the structure of BaCBS at a resolution of 2.2 A. The enzyme was found to show CBS activity only with activated serine (O-acetylserine) and not with serine, and was also observed to display OASS activity but not serine sulfhydrylase activity. BaCBS was also found to produce hydrogen sulfide (H2 S) upon reaction of cysteine and homocysteine. A mutational study revealed Glu 220, conserved in CBS, to be necessary for generating H2 S. Structurally, BaCBS display a considerably more open active site than has been found for any other CBS or OASS, which was attributed to the presence of a helix at the junction of the C- and N-terminal domains. The root-mean-square deviation (RMSD) between the backbone Calpha carbon atoms of BaCBS and those of other CBSs and OASSs were calculated to be greater than 3.0 A. The pyridoxal 5'-phosphate at the active site was not traced, and appeared to be highly flexible due to the active site being wide open. Phylogenetic analysis revealed the presence of an O-acetylserine-dependent CBS in the bacterial domain and making separate clade from CBS and OASS indicating its evolution for specific function. DATABASE: Structural data are available in the PDB under the accession number 5XW3. Structural characterization and functional analysis of cystathionine beta-synthase: an enzyme involved in the reverse transsulfuration pathway of Bacillus anthracis.,Devi S, Abdul Rehman SA, Tarique KF, Gourinath S FEBS J. 2017 Sep 16. doi: 10.1111/febs.14273. PMID:28921884[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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