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| <StructureSection load='6oux' size='340' side='right'caption='[[6oux]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='6oux' size='340' side='right'caption='[[6oux]], [[Resolution|resolution]] 1.94Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6oux]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_12446 Dsm 12446]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OUX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6oux]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurospirillum_multivorans Sulfurospirillum multivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OUX FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMUL_1544 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66821 DSM 12446])</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]] 1.94Å</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=6oux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oux OCA], [http://pdbe.org/6oux PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oux RCSB], [http://www.ebi.ac.uk/pdbsum/6oux PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oux 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=6oux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oux OCA], [https://pdbe.org/6oux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oux RCSB], [https://www.ebi.ac.uk/pdbsum/6oux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oux ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Dsm 12446]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Keller, S]] | + | [[Category: Sulfurospirillum multivorans]] |
- | [[Category: Rayment, I]] | + | [[Category: Keller S]] |
- | [[Category: Schubert, T]] | + | [[Category: Rayment I]] |
- | [[Category: Seeger, M]] | + | [[Category: Schubert T]] |
- | [[Category: Vecellio, A]] | + | [[Category: Seeger M]] |
- | [[Category: Wetterhorn, K M]] | + | [[Category: Vecellio A]] |
- | [[Category: Decarboxylase]]
| + | [[Category: Wetterhorn KM]] |
- | [[Category: Ethanolamine o-phosphate]]
| + | |
- | [[Category: Lyase]]
| + | |
- | [[Category: Smul_1544]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Structural diversity of natural cobamides (Cbas, B12 vitamers) is limited to the nucleotide loop. The loop is connected to the cobalt-containing corrin ring via an (R)-1-aminopropan-2-ol O-2-phosphate (AP-P) linker moiety. AP-P is produced by the L-threonine O-3-phosphate (L-Thr-P) decarboxylase CobD. Here, the CobD homolog SMUL_1544 of the organohalide-respiring epsilonproteobacterium Sulfurospirillum multivorans was characterized as a decarboxylase that produces ethanolamine O-phosphate (EA-P) from L-serine O-phosphate (L-Ser-P). EA-P is assumed to serve as precursor of the linker moiety of norcobamides that function as cofactors in the respiratory reductive dehalogenase. SMUL_1544 (SmCobD) is a pyridoxal-5'-phosphate (PLP)-containing enzyme. The structural analysis of the SmCobD apoprotein combined with the characterization of truncated mutant proteins uncovered a role of the SmCobD N-terminus in efficient L-Ser-P conversion. This article is protected by copyright. All rights reserved.
Structural and functional analysis of an L-serine O-phosphate decarboxylase involved in norcobamide biosynthesis.,Keller S, Wetterhorn KM, Vecellio A, Seeger M, Rayment I, Schubert T FEBS Lett. 2019 Jul 19. doi: 10.1002/1873-3468.13543. PMID:31325159[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Keller S, Wetterhorn KM, Vecellio A, Seeger M, Rayment I, Schubert T. Structural and functional analysis of an L-serine O-phosphate decarboxylase involved in norcobamide biosynthesis. FEBS Lett. 2019 Jul 19. doi: 10.1002/1873-3468.13543. PMID:31325159 doi:http://dx.doi.org/10.1002/1873-3468.13543
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