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| | <StructureSection load='5v68' size='340' side='right'caption='[[5v68]], [[Resolution|resolution]] 3.46Å' scene=''> | | <StructureSection load='5v68' size='340' side='right'caption='[[5v68]], [[Resolution|resolution]] 3.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5v68]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycta Mycta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V68 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v68]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Ra Mycobacterium tuberculosis H37Ra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V68 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.46Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsZ, MRA_2165 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=419947 MYCTA])</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v68 OCA], [http://pdbe.org/5v68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v68 RCSB], [http://www.ebi.ac.uk/pdbsum/5v68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v68 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v68 OCA], [https://pdbe.org/5v68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v68 RCSB], [https://www.ebi.ac.uk/pdbsum/5v68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v68 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FTSZ_MYCTA FTSZ_MYCTA]] 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 (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]<ref>PMID:17068335</ref> | + | [https://www.uniprot.org/uniprot/FTSZ_MYCTA FTSZ_MYCTA] 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 (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]<ref>PMID:17068335</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[Cell division protein 3D structures|Cell division protein 3D structures]] | | *[[Cell division protein 3D structures|Cell division protein 3D structures]] |
| - | *[[Journal:Acta Cryst F:S2053230X19004618|Journal:Acta Cryst F:S2053230X19004618]] | |
| | *[[Proteins from Mycobacterium tuberculosis|Proteins from Mycobacterium tuberculosis]] | | *[[Proteins from Mycobacterium tuberculosis|Proteins from Mycobacterium tuberculosis]] |
| | == References == | | == References == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycta]] | + | [[Category: Mycobacterium tuberculosis H37Ra]] |
| - | [[Category: Awasthi, D]] | + | [[Category: Awasthi D]] |
| - | [[Category: Chowdhury, S R]] | + | [[Category: Chowdhury SR]] |
| - | [[Category: Jakoncic, J]] | + | [[Category: Jakoncic J]] |
| - | [[Category: Lazo, E O]] | + | [[Category: Lazo EO]] |
| - | [[Category: Ojima, I]] | + | [[Category: Ojima I]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Gdp]]
| + | |
| - | [[Category: Mtbftsz]]
| + | |
| - | [[Category: Phosphate]]
| + | |
| - | [[Category: T9 loop]]
| + | |
| - | [[Category: Z-ring]]
| + | |
| Structural highlights
Function
FTSZ_MYCTA 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 (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909][1]
Publication Abstract from PubMed
As of 2017, tuberculosis had infected 1.7 billion people (23% of the population of the world) and caused ten million deaths. Mycobacterium tuberculosis (Mtb) is quickly evolving, and new strains are classified as multidrug resistant. Thus, the identification of novel druggable targets is essential to combat the proliferation of these drug-resistant strains. Filamenting temperature-sensitive mutant Z (FtsZ) is a key protein involved in cytokinesis, an important process for Mtb proliferation and viability. FtsZ is required for bacterial cell division because it polymerizes into a structure called the Z-ring, which recruits accessory division proteins to the septum. Here, the crystal structure of the MtbFtsZ protein has been determined to 3.46 A resolution and is described as a dimer of trimers, with an inter-subunit interface between protomers AB and DE. In this work, a novel conformation of MtbFtsZ is revealed involving the T9 loop and the nucleotide-binding pocket of protomers BC and EF.
Novel T9 loop conformation of filamenting temperature-sensitive mutant Z from Mycobacterium tuberculosis.,Lazo EO, Jakoncic J, RoyChowdhury S, Awasthi D, Ojima I Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):359-367. doi:, 10.1107/S2053230X19004618. Epub 2019 Apr 24. PMID:31045565[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thakur M, Chakraborti PK. GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA. J Biol Chem. 2006 Dec 29;281(52):40107-13. Epub 2006 Oct 26. PMID:17068335 doi:http://dx.doi.org/10.1074/jbc.M607216200
- ↑ Lazo EO, Jakoncic J, RoyChowdhury S, Awasthi D, Ojima I. Novel T9 loop conformation of filamenting temperature-sensitive mutant Z from Mycobacterium tuberculosis. Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):359-367. doi:, 10.1107/S2053230X19004618. Epub 2019 Apr 24. PMID:31045565 doi:http://dx.doi.org/10.1107/S2053230X19004618
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