2j3l
From Proteopedia
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- | [[Image:2j3l.gif|left|200px]]<br /><applet load="2j3l" size=" | + | [[Image:2j3l.gif|left|200px]]<br /><applet load="2j3l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2j3l, resolution 2.30Å" /> | caption="2j3l, resolution 2.30Å" /> | ||
'''PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)'''<br /> | '''PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 2J3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with SO4 and P5A as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] Known structural/functional Site: <scene name='pdbsite=AC1:P5a Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2J3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=P5A:'>P5A</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] Known structural/functional Site: <scene name='pdbsite=AC1:P5a+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: translation]] | [[Category: translation]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:41:09 2008'' |
Revision as of 08:41, 3 February 2008
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PROLYL-TRNA SYNTHETASE FROM ENTEROCOCCUS FAECALIS COMPLEXED WITH A PROLYL-ADENYLATE ANALOGUE ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE)
Overview
Prolyl-tRNA synthetases (ProRSs) are unique among synthetases in that they, have diverse architectures, notably the variable presence of a cis-editing, domain homologous to the freestanding deacylase proteins YbaK and ProX., Here, we describe crystal structures of two bacterial ProRSs from the, pathogen Enterococcus faecalis, which possesses an editing domain, and, from Rhodopseudomonas palustris, which does not. We compare the overall, structure and binding mode of ATP and prolyl-adenylate with those of the, archael/eukaryote-type ProRS from Thermus thermophilus. Although, structurally more homologous to YbaK, which preferentially hydrolyzes, Cys-tRNA(Pro), the editing domain of E. faecalis ProRS possesses key, elements similar to ProX, with which it shares the activity of hydrolyzing, Ala-tRNA(Pro). The structures give insight into the complex evolution of, ProRSs, the mechanism of editing, and structural differences between, prokaryotic- and eukaryotic-type ProRSs that can be exploited for, antibiotic design.
About this Structure
2J3L is a Single protein structure of sequence from Enterococcus faecalis with and as ligands. Active as Proline--tRNA ligase, with EC number 6.1.1.15 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structures of two bacterial prolyl-tRNA synthetases with and without a cis-editing domain., Crepin T, Yaremchuk A, Tukalo M, Cusack S, Structure. 2006 Oct;14(10):1511-25. PMID:17027500
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Categories: Enterococcus faecalis | Proline--tRNA ligase | Single protein | Crepin, T. | Cusack, S. | Tukalo, M. | Yaremchuk, A. | P5A | SO4 | Atp + l-proline + trna (pro) gives amp + ppi + l-prolyl-trna(pro) | Bacterial-type prolyl-trna synthetase | Class ii aminoacyl-trna synthetase | Editing | Ligase | Translation