1ah9
From Proteopedia
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| - | [[Image:1ah9.gif|left|200px]] | + | [[Image:1ah9.gif|left|200px]] |
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| - | '''THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1ah9 |SIZE=350|CAPTION= <scene name='initialview01'>1ah9</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AH9 is a [ | + | 1AH9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH9 OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif., Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi CO, Boelens R, EMBO J. 1997 Mar 17;16(6):1436-43. PMID:[http:// | + | The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif., Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi CO, Boelens R, EMBO J. 1997 Mar 17;16(6):1436-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9135158 9135158] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ribosome binding]] | [[Category: ribosome binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:57:31 2008'' |
Revision as of 07:57, 20 March 2008
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THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES
Overview
The structure of the translational initiation factor IF1 from Escherichia coli has been determined with multidimensional NMR spectroscopy. Using 1041 distance and 78 dihedral constraints, 40 distance geometry structures were calculated, which were refined by restrained molecular dynamics. From this set, 19 structures were selected, having low constraint energy and few constraint violations. The ensemble of 19 structures displays a root-mean-square deviation versus the average of 0.49 A for the backbone atoms and 1.12 A for all atoms for residues 6-36 and 46-67. The structure of IF1 is characterized by a five-stranded beta-barrel. The loop connecting strands three and four contains a short 3(10) helix but this region shows considerably higher flexibility than the beta-barrel. The fold of IF1 is very similar to that found in the bacterial cold shock proteins CspA and CspB, the N-terminal domain of aspartyl-tRNA synthetase and the staphylococcal nuclease, and can be identified as the oligomer-binding motif. Several proteins of this family are nucleic acid-binding proteins. This suggests that IF1 plays its role in the initiation of protein synthesis by nucleic acid interactions. Specific changes of NMR signals of IF1 upon titration with 30S ribosomal subunit identifies several residues that are involved in the interaction with ribosomes.
About this Structure
1AH9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif., Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi CO, Boelens R, EMBO J. 1997 Mar 17;16(6):1436-43. PMID:9135158
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