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| | <StructureSection load='1ykw' size='340' side='right'caption='[[1ykw]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1ykw' size='340' side='right'caption='[[1ykw]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ykw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_49652 Atcc 49652]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YKW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ykw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum Chlorobaculum tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YKW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CT1772 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1097 ATCC 49652])</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]] 2Å</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=1ykw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ykw OCA], [https://pdbe.org/1ykw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ykw RCSB], [https://www.ebi.ac.uk/pdbsum/1ykw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ykw 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=1ykw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ykw OCA], [https://pdbe.org/1ykw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ykw RCSB], [https://www.ebi.ac.uk/pdbsum/1ykw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ykw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RBLL_CHLTE RBLL_CHLTE]] May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity.<ref>PMID:11287671</ref> <ref>PMID:15893668</ref>
| + | [https://www.uniprot.org/uniprot/RBLL_CHLTE RBLL_CHLTE] May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity.<ref>PMID:11287671</ref> <ref>PMID:15893668</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 49652]] | + | [[Category: Chlorobaculum tepidum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eisenberg, D]] | + | [[Category: Eisenberg D]] |
| - | [[Category: Li, H]] | + | [[Category: Li H]] |
| - | [[Category: Sawaya, M R]] | + | [[Category: Sawaya MR]] |
| - | [[Category: Tabita, F R]] | + | [[Category: Tabita FR]] |
| - | [[Category: Beta-alpha-barrel]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
RBLL_CHLTE May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) catalyzes the incorporation of atmospheric CO(2) into ribulose 1,5-bisphosphate (RuBP). RuBisCOs are classified into four forms based on sequence similarity: forms I, II and III are bona fide RuBisCOs; form IV, also called the RuBisCO-like protein (RLP), lacks several of the substrate binding and catalytic residues and does not catalyze RuBP-dependent CO(2) fixation in vitro. To contribute to understanding the function of RLPs, we determined the crystal structure of the RLP from Chlorobium tepidum. The overall structure of the RLP is similar to the structures of the three other forms of RuBisCO; however, the active site is distinct from those of bona fide RuBisCOs and suggests that the RLP is possibly capable of catalyzing enolization but not carboxylation. Bioinformatic analysis of the protein functional linkages suggests that this RLP coevolved with enzymes of the bacteriochlorophyll biosynthesis pathway and may be involved in processes related to photosynthesis.
Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum.,Li H, Sawaya MR, Tabita FR, Eisenberg D Structure. 2005 May;13(5):779-89. PMID:15893668[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hanson TE, Tabita FR. A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress. Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4397-402. Epub 2001 Apr 3. PMID:11287671 doi:http://dx.doi.org/10.1073/pnas.081610398
- ↑ Li H, Sawaya MR, Tabita FR, Eisenberg D. Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum. Structure. 2005 May;13(5):779-89. PMID:15893668 doi:10.1016/j.str.2005.02.017
- ↑ Li H, Sawaya MR, Tabita FR, Eisenberg D. Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum. Structure. 2005 May;13(5):779-89. PMID:15893668 doi:10.1016/j.str.2005.02.017
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