2fsj

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(New page: 200px<br /><applet load="2fsj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fsj, resolution 1.900&Aring;" /> '''Crystal structure o...)
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[[Image:2fsj.gif|left|200px]]<br /><applet load="2fsj" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fsj.gif|left|200px]]<br /><applet load="2fsj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fsj, resolution 1.900&Aring;" />
caption="2fsj, resolution 1.900&Aring;" />
'''Crystal structure of Ta0583, an archaeal actin homolog, native data'''<br />
'''Crystal structure of Ta0583, an archaeal actin homolog, native data'''<br />
==Overview==
==Overview==
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Prokaryotic homologs of the eukaryotic structural protein actin, such as, MreB and ParM, have been implicated in determination of bacterial cell, shape, and in the segregation of genomic and plasmid DNA. In contrast to, these bacterial actin homologs, little is known about the archaeal, counterparts. As a first step, we expressed a predicted actin homolog of, the thermophilic archaeon Thermoplasma acidophilum, Ta0583, and determined, its crystal structure at 2.1A resolution. Ta0583 is expressed as a soluble, protein in T.acidophilum and is an active ATPase at physiological, temperature. In vitro, Ta0583 forms sheets with spacings resembling the, crystal lattice, indicating an inherent propensity to form filamentous, structures. The fold of Ta0583 contains the core structure of actin and, clearly belongs to the actin/Hsp70 superfamily of ATPases. Ta0583 is, approximately equidistant from actin and MreB on the structural level, and, combines features from both eubacterial actin homologs, MreB and ParM. The, structure of Ta0583 co-crystallized with ADP indicates that the nucleotide, binds at the interface between the subdomains of Ta0583 in a manner, similar to that of actin. However, the conformation of the nucleotide, observed in complex with Ta0583 clearly differs from that in complex with, actin, but closely resembles the conformation of ParM-bound nucleotide. On, the basis of sequence and structural homology, we suggest that Ta0583, derives from a ParM-like actin homolog that was once encoded by a plasmid, and was transferred into a common ancestor of Thermoplasma and, Ferroplasma. Intriguingly, both genera are characterized by the lack of a, cell wall, and therefore Ta0583 could have a function in cellular, organization.
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Prokaryotic homologs of the eukaryotic structural protein actin, such as MreB and ParM, have been implicated in determination of bacterial cell shape, and in the segregation of genomic and plasmid DNA. In contrast to these bacterial actin homologs, little is known about the archaeal counterparts. As a first step, we expressed a predicted actin homolog of the thermophilic archaeon Thermoplasma acidophilum, Ta0583, and determined its crystal structure at 2.1A resolution. Ta0583 is expressed as a soluble protein in T.acidophilum and is an active ATPase at physiological temperature. In vitro, Ta0583 forms sheets with spacings resembling the crystal lattice, indicating an inherent propensity to form filamentous structures. The fold of Ta0583 contains the core structure of actin and clearly belongs to the actin/Hsp70 superfamily of ATPases. Ta0583 is approximately equidistant from actin and MreB on the structural level, and combines features from both eubacterial actin homologs, MreB and ParM. The structure of Ta0583 co-crystallized with ADP indicates that the nucleotide binds at the interface between the subdomains of Ta0583 in a manner similar to that of actin. However, the conformation of the nucleotide observed in complex with Ta0583 clearly differs from that in complex with actin, but closely resembles the conformation of ParM-bound nucleotide. On the basis of sequence and structural homology, we suggest that Ta0583 derives from a ParM-like actin homolog that was once encoded by a plasmid and was transferred into a common ancestor of Thermoplasma and Ferroplasma. Intriguingly, both genera are characterized by the lack of a cell wall, and therefore Ta0583 could have a function in cellular organization.
==About this Structure==
==About this Structure==
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2FSJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FSJ OCA].
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2FSJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FSJ OCA].
==Reference==
==Reference==
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[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Bracher, A.]]
[[Category: Bracher, A.]]
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[[Category: Hartl, F.Ulrich.]]
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[[Category: Hartl, F Ulrich.]]
[[Category: Kofler, C.]]
[[Category: Kofler, C.]]
[[Category: Nagy, I.]]
[[Category: Nagy, I.]]
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[[Category: parm]]
[[Category: parm]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:44:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:40 2008''

Revision as of 15:24, 21 February 2008


2fsj, resolution 1.900Å

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Crystal structure of Ta0583, an archaeal actin homolog, native data

Overview

Prokaryotic homologs of the eukaryotic structural protein actin, such as MreB and ParM, have been implicated in determination of bacterial cell shape, and in the segregation of genomic and plasmid DNA. In contrast to these bacterial actin homologs, little is known about the archaeal counterparts. As a first step, we expressed a predicted actin homolog of the thermophilic archaeon Thermoplasma acidophilum, Ta0583, and determined its crystal structure at 2.1A resolution. Ta0583 is expressed as a soluble protein in T.acidophilum and is an active ATPase at physiological temperature. In vitro, Ta0583 forms sheets with spacings resembling the crystal lattice, indicating an inherent propensity to form filamentous structures. The fold of Ta0583 contains the core structure of actin and clearly belongs to the actin/Hsp70 superfamily of ATPases. Ta0583 is approximately equidistant from actin and MreB on the structural level, and combines features from both eubacterial actin homologs, MreB and ParM. The structure of Ta0583 co-crystallized with ADP indicates that the nucleotide binds at the interface between the subdomains of Ta0583 in a manner similar to that of actin. However, the conformation of the nucleotide observed in complex with Ta0583 clearly differs from that in complex with actin, but closely resembles the conformation of ParM-bound nucleotide. On the basis of sequence and structural homology, we suggest that Ta0583 derives from a ParM-like actin homolog that was once encoded by a plasmid and was transferred into a common ancestor of Thermoplasma and Ferroplasma. Intriguingly, both genera are characterized by the lack of a cell wall, and therefore Ta0583 could have a function in cellular organization.

About this Structure

2FSJ is a Single protein structure of sequence from Thermoplasma acidophilum with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of an archaeal actin homolog., Roeben A, Kofler C, Nagy I, Nickell S, Hartl FU, Bracher A, J Mol Biol. 2006 Apr 21;358(1):145-56. Epub 2006 Feb 9. PMID:16500678

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