1fsz: Difference between revisions
New page: left|200px<br /><applet load="1fsz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fsz, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1fsz.gif|left|200px]]<br /><applet load="1fsz" size=" | [[Image:1fsz.gif|left|200px]]<br /><applet load="1fsz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fsz, resolution 2.8Å" /> | caption="1fsz, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CELL-DIVISION PROTEIN FTSZ AT 2.8A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE CELL-DIVISION PROTEIN FTSZ AT 2.8A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
Bacterial cell division ends with septation, the constriction of the cell | Bacterial cell division ends with septation, the constriction of the cell wall and cell membranes that leads to the formation of two daughter cells. During septation, FtsZ, a protein of relative molecular mass 40,000 which is ubiquitous in eubacteria and is also found in archaea and chloroplasts, localizes early at the division site to form a ring-shaped septum. This septum is required for the mechanochemical process of membrane constriction. FtsZ is a GTPase with weak sequence homology to tubulins. The nature of FtsZ polymers in vivo is unknown, but FtsZ can form tubules, sheets and minirings in vitro. Here we report the crystal structure at 2.8 A resolution of recombinant FtsZ from the hyperthermophilic methanogen Methanococcus jannaschii. FtsZ has two domains, one of which is a GTPase domain with a fold related to one found in the proteins p21ras and elongation factor EF-Tu. The carboxy-terminal domain, whose function is unknown, is a four-stranded beta-sheet tilted by 90 degrees against the beta-sheet of the GTPase domain. The two domains are arranged around a central helix. GDP binding is different from that typically found in GTPases and involves four phosphate-binding loops and a sugar-binding loop in the first domain, with guanine being recognized by residues in the central connecting helix. The three-dimensional structure of FtsZ is similar to the structure of alpha- and beta-tubulin. | ||
==About this Structure== | ==About this Structure== | ||
1FSZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1FSZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSZ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Amos, L | [[Category: Amos, L A.]] | ||
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
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[[Category: tubulin]] | [[Category: tubulin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:18 2008'' | ||
Revision as of 13:42, 21 February 2008
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CRYSTAL STRUCTURE OF THE CELL-DIVISION PROTEIN FTSZ AT 2.8A RESOLUTION
OverviewOverview
Bacterial cell division ends with septation, the constriction of the cell wall and cell membranes that leads to the formation of two daughter cells. During septation, FtsZ, a protein of relative molecular mass 40,000 which is ubiquitous in eubacteria and is also found in archaea and chloroplasts, localizes early at the division site to form a ring-shaped septum. This septum is required for the mechanochemical process of membrane constriction. FtsZ is a GTPase with weak sequence homology to tubulins. The nature of FtsZ polymers in vivo is unknown, but FtsZ can form tubules, sheets and minirings in vitro. Here we report the crystal structure at 2.8 A resolution of recombinant FtsZ from the hyperthermophilic methanogen Methanococcus jannaschii. FtsZ has two domains, one of which is a GTPase domain with a fold related to one found in the proteins p21ras and elongation factor EF-Tu. The carboxy-terminal domain, whose function is unknown, is a four-stranded beta-sheet tilted by 90 degrees against the beta-sheet of the GTPase domain. The two domains are arranged around a central helix. GDP binding is different from that typically found in GTPases and involves four phosphate-binding loops and a sugar-binding loop in the first domain, with guanine being recognized by residues in the central connecting helix. The three-dimensional structure of FtsZ is similar to the structure of alpha- and beta-tubulin.
About this StructureAbout this Structure
1FSZ is a Single protein structure of sequence from Methanocaldococcus jannaschii with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the bacterial cell-division protein FtsZ., Lowe J, Amos LA, Nature. 1998 Jan 8;391(6663):203-6. PMID:9428770
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