1rqg

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[[Image:1rqg.gif|left|200px]]<br /><applet load="1rqg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rqg.gif|left|200px]]
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caption="1rqg, resolution 2.9&Aring;" />
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'''Methionyl-tRNA synthetase from Pyrococcus abyssi'''<br />
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{{Structure
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|PDB= 1rqg |SIZE=350|CAPTION= <scene name='initialview01'>1rqg</scene>, resolution 2.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [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]
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|GENE= METG, METS, PYRAB09870, PAB2364 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi])
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}}
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'''Methionyl-tRNA synthetase from Pyrococcus abyssi'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RQG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQG OCA].
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1RQG 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=1RQG OCA].
==Reference==
==Reference==
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Three-dimensional structure of methionyl-tRNA synthetase from Pyrococcus abyssi., Crepin T, Schmitt E, Blanquet S, Mechulam Y, Biochemistry. 2004 Mar 9;43(9):2635-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14992601 14992601]
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Three-dimensional structure of methionyl-tRNA synthetase from Pyrococcus abyssi., Crepin T, Schmitt E, Blanquet S, Mechulam Y, Biochemistry. 2004 Mar 9;43(9):2635-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14992601 14992601]
[[Category: Methionine--tRNA ligase]]
[[Category: Methionine--tRNA ligase]]
[[Category: Pyrococcus abyssi]]
[[Category: Pyrococcus abyssi]]
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[[Category: translation]]
[[Category: translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:55:01 2008''

Revision as of 11:55, 20 March 2008


PDB ID 1rqg

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands:
Gene: METG, METS, PYRAB09870, PAB2364 (Pyrococcus abyssi)
Activity: Methionine--tRNA ligase, with EC number 6.1.1.10
Coordinates: save as pdb, mmCIF, xml



Methionyl-tRNA synthetase from Pyrococcus abyssi


Overview

In class 1 aminoacyl-tRNA synthetases, methionyl-tRNA synthetases (MetRS) are homodimers or monomers depending on the presence or absence of a domain appended at the C-side of the polypeptide chain. Beyond this C-domain, all MetRS display a highly conserved catalytic core with a Rossmann fold, the two halves of which are linked by a connective peptide (CP). Three-dimensional folding of CP and its putative zinc content have served as a basis to propose a division of the MetRS family into four subgroups. All subgroups but one, which is predicted to display two zincs per MetRS polypeptide, have been characterized. In the present study, the 3D structure of MetRS from Pyrococcus abyssi could be solved at 2.9 A resolution. The data obtained and atomic absorption spectroscopic measurements establish the presence of two metal ions per polypeptide chain. This finding brings strong support to the above classification. In the crystal, the C-terminal dimerization domain is disordered. This observation is thought to reflect marked flexibility of the two core moieties with respect to the C-domains in the dimer. Gel shift experiments were performed with the isolated C-terminal dimerization domain and a core monomeric MetRS, both derived from the P. abyssi enzyme. Complex formation between the C-domain and the core enzyme could not be evidenced. Moreover, association of tRNA(Met) to the core enzyme is enhanced in the presence of the C-domain. Together, these experiments suggest positive control in trans by the C-domain on recognition of tRNA by the core moiety of MetRS.

About this Structure

1RQG is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of methionyl-tRNA synthetase from Pyrococcus abyssi., Crepin T, Schmitt E, Blanquet S, Mechulam Y, Biochemistry. 2004 Mar 9;43(9):2635-44. PMID:14992601

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