2j69

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(New page: 200px<br /><applet load="2j69" size="350" color="white" frame="true" align="right" spinBox="true" caption="2j69, resolution 3.00&Aring;" /> '''BACTERIAL DYNAMIN-LI...)
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==Overview==
==Overview==
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Dynamins form a superfamily of large mechano-chemical GTPases that, includes the classical dynamins and dynamin-like proteins (DLPs). They are, found throughout the Eukarya, functioning in core cellular processes such, as endocytosis and organelle division. Many bacteria are predicted by, sequence to possess large GTPases with the same multidomain architecture, that is found in DLPs. Mechanistic dissection of dynamin family members, has been impeded by a lack of high-resolution structural data currently, restricted to the GTPase and pleckstrin homology domains, and the, dynamin-related human guanylate-binding protein. Here we present the, crystal structure of a cyanobacterial DLP in both nucleotide-free and, GDP-associated conformation. The bacterial DLP shows dynamin-like, qualities, such as helical self-assembly and tubulation of a lipid, bilayer. In vivo, it localizes to the membrane in a manner reminiscent of, FZL, a chloroplast-specific dynamin-related protein with which it shares, sequence similarity. Our results provide structural and mechanistic, insight that may be relevant across the dynamin superfamily. Concurrently, we show compelling similarity between a cyanobacterial and chloroplast DLP, that, given the endosymbiotic ancestry of chloroplasts, questions the, evolutionary origins of dynamins.
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Dynamins form a superfamily of large mechano-chemical GTPases that includes the classical dynamins and dynamin-like proteins (DLPs). They are found throughout the Eukarya, functioning in core cellular processes such as endocytosis and organelle division. Many bacteria are predicted by sequence to possess large GTPases with the same multidomain architecture that is found in DLPs. Mechanistic dissection of dynamin family members has been impeded by a lack of high-resolution structural data currently restricted to the GTPase and pleckstrin homology domains, and the dynamin-related human guanylate-binding protein. Here we present the crystal structure of a cyanobacterial DLP in both nucleotide-free and GDP-associated conformation. The bacterial DLP shows dynamin-like qualities, such as helical self-assembly and tubulation of a lipid bilayer. In vivo, it localizes to the membrane in a manner reminiscent of FZL, a chloroplast-specific dynamin-related protein with which it shares sequence similarity. Our results provide structural and mechanistic insight that may be relevant across the dynamin superfamily. Concurrently, we show compelling similarity between a cyanobacterial and chloroplast DLP that, given the endosymbiotic ancestry of chloroplasts, questions the evolutionary origins of dynamins.
==About this Structure==
==About this Structure==
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[[Category: Nostoc punctiforme]]
[[Category: Nostoc punctiforme]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Low, H.H.]]
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[[Category: Low, H H.]]
[[Category: Lowe, J.]]
[[Category: Lowe, J.]]
[[Category: dynamin]]
[[Category: dynamin]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:51:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:46 2008''

Revision as of 15:59, 21 February 2008

Image:2j69.jpg

2j69, resolution 3.00Å

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BACTERIAL DYNAMIN-LIKE PROTEIN BDLP

Overview

Dynamins form a superfamily of large mechano-chemical GTPases that includes the classical dynamins and dynamin-like proteins (DLPs). They are found throughout the Eukarya, functioning in core cellular processes such as endocytosis and organelle division. Many bacteria are predicted by sequence to possess large GTPases with the same multidomain architecture that is found in DLPs. Mechanistic dissection of dynamin family members has been impeded by a lack of high-resolution structural data currently restricted to the GTPase and pleckstrin homology domains, and the dynamin-related human guanylate-binding protein. Here we present the crystal structure of a cyanobacterial DLP in both nucleotide-free and GDP-associated conformation. The bacterial DLP shows dynamin-like qualities, such as helical self-assembly and tubulation of a lipid bilayer. In vivo, it localizes to the membrane in a manner reminiscent of FZL, a chloroplast-specific dynamin-related protein with which it shares sequence similarity. Our results provide structural and mechanistic insight that may be relevant across the dynamin superfamily. Concurrently, we show compelling similarity between a cyanobacterial and chloroplast DLP that, given the endosymbiotic ancestry of chloroplasts, questions the evolutionary origins of dynamins.

About this Structure

2J69 is a Single protein structure of sequence from Nostoc punctiforme. Full crystallographic information is available from OCA.

Reference

A bacterial dynamin-like protein., Low HH, Lowe J, Nature. 2006 Dec 7;444(7120):766-9. Epub 2006 Nov 22. PMID:17122778

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