1fsz: Difference between revisions

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-[[Image:1fsz.gif|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE CELL-DIVISION PROTEIN FTSZ AT 2.8A RESOLUTION==
-The line below this paragraph, containing "STRUCTURE_1fsz", creates the "Structure Box" on the page.
+<StructureSection load='1fsz' size='340' side='right'caption='[[1fsz]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1fsz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FSZ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
-{{STRUCTURE_1fsz|  PDB=1fsz  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fsz OCA], [https://pdbe.org/1fsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fsz RCSB], [https://www.ebi.ac.uk/pdbsum/1fsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fsz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FTSZ1_METJA FTSZ1_METJA] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (By similarity).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fs/1fsz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fsz ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF THE CELL-DIVISION PROTEIN FTSZ AT 2.8A RESOLUTION'''
+==See Also==
+*[[Cell division protein 3D structures|Cell division protein 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-FSZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSZ OCA].
-==Reference==
-Crystal structure of the bacterial cell-division protein FtsZ., Lowe J, Amos LA, Nature. 1998 Jan 8;391(6663):203-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9428770 9428770]
 [[Category: Methanocaldococcus jannaschii]]
-[[Category: Single protein]]
+[[Category: Amos LA]]
-[[Category: Amos, L A.]]
+[[Category: Lowe J]]
-[[Category: Lowe, J.]]
-[[Category: Cell division protein]]
-[[Category: Ftsz]]
-[[Category: Tubulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:43:57 2008''