1mkh

<StructureSection load='1mkh' size='340' side='right' caption='[[1mkh]], [[Resolution|resolution]] 2.01&Aring;' scene=''>

<table><tr><td colspan='2'>[[1mkh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKH FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 "Pyrococcus abyssi" Erauso et al. 1993])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=1mkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkh OCA], [http://pdbe.org/1mkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mkh RCSB], [http://www.ebi.ac.uk/pdbsum/1mkh PDBsum]</span></td></tr>

[[http://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).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mk/1mkh_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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:12390027<ref>PMID:12390027</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mkh" style="background-color:#fffaf0;"></div>

*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]

[[Category: Pyrococcus abyssi erauso et al. 1993]]

[[Category: Methionine--tRNA ligase]]

[[Category: Blanquet, S]]

[[Category: Crepin, T]]

[[Category: Mechulam, Y]]

[[Category: Schmitt, E]]

[[Category: Ligase]]