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| ==NMR structure of IF1 from Pseudomonas aeruginosa== | | ==NMR structure of IF1 from Pseudomonas aeruginosa== |
- | <StructureSection load='2n78' size='340' side='right' caption='[[2n78]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2n78' size='340' side='right'caption='[[2n78]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2n78]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N78 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n78]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N78 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">infA, ERS445055_02430, PA257_2936, PA8380_26730, PAMH19_6240, YQ19_15045 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">infA, ERS445055_02430, PA257_2936, PA8380_26730, PAMH19_6240, YQ19_15045 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=2n78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n78 OCA], [http://pdbe.org/2n78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n78 RCSB], [http://www.ebi.ac.uk/pdbsum/2n78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n78 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=2n78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n78 OCA], [https://pdbe.org/2n78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n78 RCSB], [https://www.ebi.ac.uk/pdbsum/2n78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n78 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/A0A072ZPH3_PSEAI A0A072ZPH3_PSEAI]] 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 initation complex.[HAMAP-Rule:MF_00075][SAAS:SAAS00571771] | + | [[https://www.uniprot.org/uniprot/A0A072ZPH3_PSEAI A0A072ZPH3_PSEAI]] 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 initation complex.[HAMAP-Rule:MF_00075][SAAS:SAAS00571771] |
| <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: Large Structures]] |
| [[Category: Zhang, Y]] | | [[Category: Zhang, Y]] |
| [[Category: Translation]] | | [[Category: Translation]] |
| Structural highlights
2n78 is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Gene: | infA, ERS445055_02430, PA257_2936, PA8380_26730, PAMH19_6240, YQ19_15045 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[A0A072ZPH3_PSEAI] 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 initation complex.[HAMAP-Rule:MF_00075][SAAS:SAAS00571771]
Publication Abstract from PubMed
Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen and a primary cause of infection in humans. P. aeruginosa can acquire resistance against multiple groups of antimicrobial agents, including beta-lactams, aminoglycosides and fluoroquinolones, and multidrug resistance is increasing in this organism which makes treatment of the infections difficult and expensive. This has led to the unmet need for discovery of new compounds distinctly different from present antimicrobials. Protein synthesis is an essential metabolic process and a validated target for the development of new antibiotics. Translation initiation factor 1 from P. aeruginosa (Pa-IF1) is the smallest of the three initiation factors that acts to establish the 30S initiation complex to initiate translation during protein biosynthesis, and its structure is unknown. Here we report the 1H, 13C and 15N chemical shift assignments of Pa-IF1 as the basis for NMR structure determination and interaction studies. Secondary structure analyses deduced from the NMR chemical shift data have identified five beta-strands with an unusually extended beta-strand at the C-terminal end of the protein and one short alpha-helix arranged in the sequential order beta1-beta2-beta3-alpha1-beta4-beta5. This is further supported by 15N-{1H} hetero NOEs. These secondary structure elements suggest the Pa-IF1 adopts the typical beta-barrel structure and is composed of an oligomer-binding motif.
1H, 13C and 15N resonance assignments and secondary structure analysis of translation initiation factor 1 from Pseudomonas aeruginosa.,Bernal A, Hu Y, Palmer SO, Silva A, Bullard J, Zhang Y Biomol NMR Assign. 2016 Mar 16. PMID:26983940[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernal A, Hu Y, Palmer SO, Silva A, Bullard J, Zhang Y. 1H, 13C and 15N resonance assignments and secondary structure analysis of translation initiation factor 1 from Pseudomonas aeruginosa. Biomol NMR Assign. 2016 Mar 16. PMID:26983940 doi:http://dx.doi.org/10.1007/s12104-016-9678-7
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