1jcf: Difference between revisions
New page: left|200px<br /><applet load="1jcf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jcf, resolution 2.1Å" /> '''MREB FROM THERMOTOGA ... |
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[[Image:1jcf.gif|left|200px]]<br /><applet load="1jcf" size=" | [[Image:1jcf.gif|left|200px]]<br /><applet load="1jcf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jcf, resolution 2.1Å" /> | caption="1jcf, resolution 2.1Å" /> | ||
'''MREB FROM THERMOTOGA MARITIMA, TRIGONAL'''<br /> | '''MREB FROM THERMOTOGA MARITIMA, TRIGONAL'''<br /> | ||
==Overview== | ==Overview== | ||
It was thought until recently that bacteria lack the actin or tubulin | It was thought until recently that bacteria lack the actin or tubulin filament networks that organize eukaryotic cytoplasm. However, we show here that the bacterial MreB protein assembles into filaments with a subunit repeat similar to that of F-actin-the physiological polymer of eukaryotic actin. By elucidating the MreB crystal structure we demonstrate that MreB and actin are very similar in three dimensions. Moreover, the crystals contain protofilaments, allowing visualization of actin-like strands at atomic resolution. The structure of the MreB protofilament is in remarkably good agreement with the model for F-actin, showing that the proteins assemble in identical orientations. The actin-like properties of MreB explain the finding that MreB forms large fibrous spirals under the cell membrane of rod-shaped cells, where they are involved in cell-shape determination. Thus, prokaryotes are now known to possess homologues both of tubulin, namely FtsZ, and of actin. | ||
==About this Structure== | ==About this Structure== | ||
1JCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http:// | 1JCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCF OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Amos, L | [[Category: Amos, L A.]] | ||
[[Category: Ent, F | [[Category: Ent, F van den.]] | ||
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: actin]] | [[Category: actin]] | ||
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[[Category: rod-shape determining]] | [[Category: rod-shape determining]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:03 2008'' | ||
Revision as of 14:21, 21 February 2008
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MREB FROM THERMOTOGA MARITIMA, TRIGONAL
OverviewOverview
It was thought until recently that bacteria lack the actin or tubulin filament networks that organize eukaryotic cytoplasm. However, we show here that the bacterial MreB protein assembles into filaments with a subunit repeat similar to that of F-actin-the physiological polymer of eukaryotic actin. By elucidating the MreB crystal structure we demonstrate that MreB and actin are very similar in three dimensions. Moreover, the crystals contain protofilaments, allowing visualization of actin-like strands at atomic resolution. The structure of the MreB protofilament is in remarkably good agreement with the model for F-actin, showing that the proteins assemble in identical orientations. The actin-like properties of MreB explain the finding that MreB forms large fibrous spirals under the cell membrane of rod-shaped cells, where they are involved in cell-shape determination. Thus, prokaryotes are now known to possess homologues both of tubulin, namely FtsZ, and of actin.
About this StructureAbout this Structure
1JCF is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
Prokaryotic origin of the actin cytoskeleton., van den Ent F, Amos LA, Lowe J, Nature. 2001 Sep 6;413(6851):39-44. PMID:11544518
Page seeded by OCA on Thu Feb 21 13:21:03 2008