| General information | | DisProt: | DP00021 | | Name: | Elongation factor G | | Synonym(s): | EFG_THETH
EF-G
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P13551 | | UniGene: | | | SwissProt: | EFG_THETH | | TrEMBL: | | | NCBI (GI): | 119190 | | Source organism: | Thermus thermophilus | | Sequence length: | 691 | | Percent disordered: | 4% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA TMDFMEQERE - 60
RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV LDGAIVVFDS SQGVEPQSET - 120
VWRQAEKYKV PRIAFANKMD KTGADLWLVI RTMQERLGAR PVVMQLPIGR EDTFSGIIDV - 180
LRMKAYTYGN DLGTDIREIP IPEEYLDQAR EYHEKLVEVA ADFDENIMLK YLEGEEPTEE - 240
ELVAAIRKGT IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE - 300
IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE RVARLLRMHA - 360
NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE SIEVPEPVID VAIEPKTKAD - 420
QEKLSQALAR LAEEDPTFRV STHPETGQTI ISGMGELHLE IIVDRLKREF KVDANVGKPQ - 480
VAYRETITKP VDVEGKFIRQ TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP - 540
AVQKGIEEAM QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV - 600
ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA EMFGYATDLR - 660
SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q
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| Functional narrative |
This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. HAMAP MF_00054_B
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 40 - 65 | | Length: | 26 | | Region sequence: |
HKIGEVHEGAATMDFMEQERERGITI | | Modification type: | Mutant
| | PDB: | 1FNM:A | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Protein-tRNA binding
Substrate/ligand binding
| Detection methods:
- X-ray crystallography (pH: 7.4; resolution 2.8 A; wavelength 0.935 A; GDP 0.5 mM; glycerol (v/v) 25 %)
| References:
- Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A. "Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site." J Mol Biol. 2000; 303(4): 593-603. PubMed: 11054294
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | effector region | | Location: | 38 - 68 | | Length: | 31 | | Region sequence: |
RIHKIGEVHEGAATMDFMEQERERGITITAA | | Modification type: | Mutant
| | PDB: | 1FNM:A | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Protein-tRNA binding
Substrate/ligand binding
| Detection methods:
- X-ray crystallography (pH: 7.4; GDP 0.5 mM; glycerol (v/v) 25 %; resolution 2.8 A; wavelength 0.935 A)
| References:
- AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A. "Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus." EMBO J. 1994; 13(16): 3669-77. PubMed: 8070397
- Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A. "Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site." J Mol Biol. 2000; 303(4): 593-603. PubMed: 11054294
| Comments:
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| References |
- AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A. "Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus." EMBO J. 1994; 13(16): 3669-77. PubMed: 8070397
- Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A. "Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site." J Mol Biol. 2000; 303(4): 593-603. PubMed: 11054294
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| Comments |
Sent for AV (6-15-2010) PubMed: 8070397
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