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| | ==Solution structure of translation initiation factor 1 from Clostridium difficile== | | ==Solution structure of translation initiation factor 1 from Clostridium difficile== |
| - | <StructureSection load='6c00' size='340' side='right'caption='[[6c00]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='6c00' size='340' side='right'caption='[[6c00]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c00]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C00 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c00]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C00 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">infA, CD630_00940 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</td></tr> | + | </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=6c00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c00 OCA], [https://pdbe.org/6c00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c00 RCSB], [https://www.ebi.ac.uk/pdbsum/6c00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c00 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=6c00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c00 OCA], [http://pdbe.org/6c00 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c00 RCSB], [http://www.ebi.ac.uk/pdbsum/6c00 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c00 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IF1_PEPD6 IF1_PEPD6]] One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. | + | [https://www.uniprot.org/uniprot/IF1_CLOD6 IF1_CLOD6] One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.[HAMAP-Rule:MF_00075] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus difficilis hall and o'toole 1935]] | + | [[Category: Clostridioides difficile]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aguilar, F]] | + | [[Category: Aguilar F]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Zhang Y]] |
| - | [[Category: Translation]]
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| - | [[Category: Translation initiation factor]]
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| Structural highlights
Function
IF1_CLOD6 One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.[HAMAP-Rule:MF_00075]
Publication Abstract from PubMed
Clostridium difficile is a gram-positive, toxin-producing, anaerobic bacterium whose virulence factors and mechanisms of pathogenesis require further investigation. C. difficile infections (CDI) result in the severe and potentially fatal gastrointestinal diseases pseudomembranous colitis and toxic megacolon following extensive broad spectrum antibiotic treatment. The increasing C. difficile fatalities are a result of the bacteria's growing antibiotic resistance and consequential CDI recurrence, which led to the unmet need for new CDI treatment. Bacterial protein synthesis is an essential metabolic process and an effective target for antibacterial agents. Translation initiation factor 1 from C. difficile (Cd-IF1) is the smallest of the three initiation factors that acts to establish the 30S initiation complex to initiate translation during protein biosynthesis. Here we report the complete NMR (1)H, (13)C and (15)N chemical shift assignments of Cd-IF1 as the basis for NMR structure determination and interaction studies. Secondary structure analyses have identified five beta-strands and one short alpha-helix arranged in the sequential order beta1-beta2-beta3-alpha1-beta4-beta5, which is supported by (15)N-{(1)H} heteroNOEs. The assigned chemical shifts were used to conduct structure prediction by CS-Rosetta. The predicted structure suggests that Cd-IF1 adopts the typical beta-barrel structure and is composed of an oligomer-binding motif.
(1)H, (13)C and (15)N resonance assignments and structure prediction of translation initiation factor 1 from Clostridium difficile.,Aguilar F, Banaei N, Zhang Y Biomol NMR Assign. 2019 Apr;13(1):91-95. doi: 10.1007/s12104-018-9858-8. Epub, 2018 Oct 28. PMID:30370502[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aguilar F, Banaei N, Zhang Y. (1)H, (13)C and (15)N resonance assignments and structure prediction of translation initiation factor 1 from Clostridium difficile. Biomol NMR Assign. 2019 Apr;13(1):91-95. doi: 10.1007/s12104-018-9858-8. Epub, 2018 Oct 28. PMID:30370502 doi:http://dx.doi.org/10.1007/s12104-018-9858-8
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