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1mkh

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[[Image:1mkh.jpg|left|200px]]
 
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{{Structure
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==C-terminal domain of methionyl-tRNA synthetase from Pyrococcus abyssi==
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|PDB= 1mkh |SIZE=350|CAPTION= <scene name='initialview01'>1mkh</scene>, resolution 2.01&Aring;
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<StructureSection load='1mkh' size='340' side='right'caption='[[1mkh]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1mkh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKH FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
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|GENE= metG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkh OCA], [https://pdbe.org/1mkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mkh RCSB], [https://www.ebi.ac.uk/pdbsum/1mkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mkh ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkh OCA], [http://www.ebi.ac.uk/pdbsum/1mkh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mkh RCSB]</span>
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[https://www.uniprot.org/uniprot/SYM_PYRAB SYM_PYRAB] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (By similarity).
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mk/1mkh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mkh ConSurf].
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<div style="clear:both"></div>
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'''C-terminal domain of methionyl-tRNA synthetase from Pyrococcus abyssi'''
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==See Also==
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The minimal polypeptide supporting full methionyl-tRNA synthetase (MetRS) activity is composed of four domains: a catalytic Rossmann fold, a connective peptide, a KMSKS domain, and a C-terminal alpha helix bundle domain. The minimal MetRS behaves as a monomer. In several species, MetRS is a homodimer because of a C-terminal domain appended to the core polypeptide. Upon truncation of this C-terminal domain, subunits dissociate irreversibly. Here, the C-terminal domain of dimeric MetRS from Pyrococcus abyssi was isolated and studied. It displays nonspecific tRNA-binding properties and has a crystalline structure closely resembling that of Trbp111, a dimeric tRNA-binding protein found in many bacteria and archaea. The obtained 3D model was used to direct mutations against dimerization of Escherichia coli MetRS. Comparison of the resulting mutants to native and C-truncated MetRS shows that the presence of the appended C-domain improves tRNA(Met) binding affinity. However, dimer formation is required to evidence the gain in affinity.
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[[Category: Large Structures]]
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==About this Structure==
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1MKH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKH OCA].
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==Reference==
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Structure and function of the C-terminal domain of methionyl-tRNA synthetase., Crepin T, Schmitt E, Blanquet S, Mechulam Y, Biochemistry. 2002 Oct 29;41(43):13003-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12390027 12390027]
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[[Category: Methionine--tRNA ligase]]
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[[Category: Pyrococcus abyssi]]
[[Category: Pyrococcus abyssi]]
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[[Category: Single protein]]
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[[Category: Blanquet S]]
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[[Category: Blanquet, S.]]
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[[Category: Crepin T]]
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[[Category: Crepin, T.]]
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[[Category: Mechulam Y]]
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[[Category: Mechulam, Y.]]
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[[Category: Schmitt E]]
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[[Category: Schmitt, E.]]
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[[Category: beta barrel]]
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[[Category: dimerization domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:17:19 2008''
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Current revision

C-terminal domain of methionyl-tRNA synthetase from Pyrococcus abyssi

PDB ID 1mkh

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