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| - | '''Unreleased structure''' | |
| | | | |
| - | The entry 9h9j is ON HOLD until Paper Publication
| + | ==Complex 2 (BODY) 30S-IF1-IF3-tRNA-GE81112== |
| - | | + | <StructureSection load='9h9j' size='340' side='right'caption='[[9h9j]], [[Resolution|resolution]] 3.20Å' scene=''> |
| - | Authors: Schedlbauer, A., Han, X., van Bakel, W., Kaminishi, T., Ochoa-Lizarralde, B., Iturrioz, I., Capuni, R., Parry, R., Zegarra, R., Gil-Carton, D., Lopez-Alonso, J.P., Barragan Sanz, K., Brandi, L., Gualerzi, C.O., Fucini, P., Connell, S.R.
| + | == Structural highlights == |
| - | | + | <table><tr><td colspan='2'>[[9h9j]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9H9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H9J FirstGlance]. <br> |
| - | Description: Complex 2 (BODY) 30S-IF1-IF3-tRNA-GE81112
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | [[Category: Unreleased Structures]] | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MG:2N-METHYLGUANOSINE-5-MONOPHOSPHATE'>2MG</scene>, <scene name='pdbligand=4OC:4N,O2-METHYLCYTIDINE-5-MONOPHOSPHATE'>4OC</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=A1IC4:(2~{S},3~{S})-2-[[(2~{S})-2-[[(2~{S},4~{S})-5-aminocarbonyloxy-4-oxidanyl-2-[[(2~{S},3~{R})-3-oxidanylpiperidin-2-yl]carbonylamino]pentanoyl]amino]-3-(1~{H}-imidazol-4-yl)propanoyl]amino]-3-(2-chloranyl-1~{H}-imidazol-4-yl)-3-oxidanyl-propanoic+acid'>A1IC4</scene>, <scene name='pdbligand=G7M:N7-METHYL-GUANOSINE-5-MONOPHOSPHATE'>G7M</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'>MA6</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=UR3:3-METHYLURIDINE-5-MONOPHOSHATE'>UR3</scene></td></tr> |
| - | [[Category: Schedlbauer, A]] | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9h9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h9j OCA], [https://pdbe.org/9h9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h9j RCSB], [https://www.ebi.ac.uk/pdbsum/9h9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h9j ProSAT]</span></td></tr> |
| - | [[Category: Han, X]] | + | </table> |
| - | [[Category: Fucini, P]] | + | == Function == |
| - | [[Category: Kaminishi, T]] | + | [https://www.uniprot.org/uniprot/RS4_ECOLI RS4_ECOLI] One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.<ref>PMID:2461734</ref> <ref>PMID:11447122</ref> <ref>PMID:15652481</ref> With S5 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).<ref>PMID:2461734</ref> <ref>PMID:11447122</ref> <ref>PMID:15652481</ref> Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.<ref>PMID:2461734</ref> <ref>PMID:11447122</ref> <ref>PMID:15652481</ref> Protein S4 is also a translational repressor protein, it controls the translation of the alpha-operon (which codes for S13, S11, S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA.<ref>PMID:2461734</ref> <ref>PMID:11447122</ref> <ref>PMID:15652481</ref> Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase.<ref>PMID:2461734</ref> <ref>PMID:11447122</ref> <ref>PMID:15652481</ref> |
| - | [[Category: Gil-Carton, D]] | + | == References == |
| - | [[Category: Van Bakel, W]] | + | <references/> |
| - | [[Category: Gualerzi, C.O]] | + | __TOC__ |
| - | [[Category: Iturrioz, I]] | + | </StructureSection> |
| - | [[Category: Lopez-Alonso, J.P]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Capuni, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Barragan Sanz, K]] | + | [[Category: Barragan Sanz K]] |
| - | [[Category: Ochoa-Lizarralde, B]] | + | [[Category: Brandi L]] |
| - | [[Category: Brandi, L]] | + | [[Category: Capuni R]] |
| - | [[Category: Parry, R]] | + | [[Category: Connell SR]] |
| - | [[Category: Zegarra, R]] | + | [[Category: Fucini P]] |
| - | [[Category: Connell, S.R]] | + | [[Category: Gil-Carton D]] |
| | + | [[Category: Gualerzi CO]] |
| | + | [[Category: Han X]] |
| | + | [[Category: Iturrioz I]] |
| | + | [[Category: Kaminishi T]] |
| | + | [[Category: Lopez-Alonso JP]] |
| | + | [[Category: Ochoa-Lizarralde B]] |
| | + | [[Category: Parry R]] |
| | + | [[Category: Schedlbauer A]] |
| | + | [[Category: Zegarra R]] |
| | + | [[Category: Van Bakel W]] |
| Structural highlights
9h9j is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | Electron Microscopy, Resolution 3.2Å |
| Ligands: | , , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
RS4_ECOLI One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.[1] [2] [3] With S5 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).[4] [5] [6] Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.[7] [8] [9] Protein S4 is also a translational repressor protein, it controls the translation of the alpha-operon (which codes for S13, S11, S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA.[10] [11] [12] Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase.[13] [14] [15]
References
- ↑ Nowotny V, Nierhaus KH. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. PMID:2461734
- ↑ Torres M, Condon C, Balada JM, Squires C, Squires CL. Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 2001 Jul 16;20(14):3811-20. PMID:11447122 doi:10.1093/emboj/20.14.3811
- ↑ Takyar S, Hickerson RP, Noller HF. mRNA helicase activity of the ribosome. Cell. 2005 Jan 14;120(1):49-58. PMID:15652481 doi:10.1016/j.cell.2004.11.042
- ↑ Nowotny V, Nierhaus KH. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. PMID:2461734
- ↑ Torres M, Condon C, Balada JM, Squires C, Squires CL. Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 2001 Jul 16;20(14):3811-20. PMID:11447122 doi:10.1093/emboj/20.14.3811
- ↑ Takyar S, Hickerson RP, Noller HF. mRNA helicase activity of the ribosome. Cell. 2005 Jan 14;120(1):49-58. PMID:15652481 doi:10.1016/j.cell.2004.11.042
- ↑ Nowotny V, Nierhaus KH. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. PMID:2461734
- ↑ Torres M, Condon C, Balada JM, Squires C, Squires CL. Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 2001 Jul 16;20(14):3811-20. PMID:11447122 doi:10.1093/emboj/20.14.3811
- ↑ Takyar S, Hickerson RP, Noller HF. mRNA helicase activity of the ribosome. Cell. 2005 Jan 14;120(1):49-58. PMID:15652481 doi:10.1016/j.cell.2004.11.042
- ↑ Nowotny V, Nierhaus KH. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. PMID:2461734
- ↑ Torres M, Condon C, Balada JM, Squires C, Squires CL. Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 2001 Jul 16;20(14):3811-20. PMID:11447122 doi:10.1093/emboj/20.14.3811
- ↑ Takyar S, Hickerson RP, Noller HF. mRNA helicase activity of the ribosome. Cell. 2005 Jan 14;120(1):49-58. PMID:15652481 doi:10.1016/j.cell.2004.11.042
- ↑ Nowotny V, Nierhaus KH. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. PMID:2461734
- ↑ Torres M, Condon C, Balada JM, Squires C, Squires CL. Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 2001 Jul 16;20(14):3811-20. PMID:11447122 doi:10.1093/emboj/20.14.3811
- ↑ Takyar S, Hickerson RP, Noller HF. mRNA helicase activity of the ribosome. Cell. 2005 Jan 14;120(1):49-58. PMID:15652481 doi:10.1016/j.cell.2004.11.042
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