|
|
| (11 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
| [[Image:2h3g.jpg|left|200px]]
| |
|
| |
|
| {{Structure
| | ==Structure of the Type III Pantothenate Kinase (CoaX) from Bacillus Anthracis== |
| |PDB= 2h3g |SIZE=350|CAPTION= <scene name='initialview01'>2h3g</scene>, resolution 2.000Å
| | <StructureSection load='2h3g' size='340' side='right'caption='[[2h3g]], [[Resolution|resolution]] 2.00Å' scene=''> |
| |SITE= | | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=EGL:ETHYLENE+GLYCOL'>EGL</scene>
| | <table><tr><td colspan='2'>[[2h3g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Ames Bacillus anthracis str. Ames]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H3G FirstGlance]. <br> |
| |ACTIVITY=
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| |GENE=
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| |DOMAIN=
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3g OCA], [https://pdbe.org/2h3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h3g RCSB], [https://www.ebi.ac.uk/pdbsum/2h3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h3g ProSAT]</span></td></tr> |
| |RELATEDENTRY=
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3g OCA], [http://www.ebi.ac.uk/pdbsum/2h3g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h3g RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/COAX_BACAN COAX_BACAN] Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.[HAMAP-Rule:MF_01274] |
| | == 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/h3/2h3g_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=2h3g ConSurf]. |
| | <div style="clear:both"></div> |
|
| |
|
| '''Structure of the Type III Pantothenate Kinase (CoaX) from Bacillus Anthracis'''
| | ==See Also== |
| | | *[[Pantothenate kinase 3D structures|Pantothenate kinase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| Coenzyme A (CoASH) is the major low-molecular weight thiol in Staphylococcus aureus and a number of other bacteria; the crystal structure of the S. aureus coenzyme A-disulfide reductase (CoADR), which maintains the reduced intracellular state of CoASH, has recently been reported [Mallett, T.C., Wallen, J.R., Karplus, P.A., Sakai, H., Tsukihara, T., and Claiborne, A. (2006) Biochemistry 45, 11278-89]. In this report we demonstrate that CoASH is the major thiol in Bacillus anthracis; a bioinformatics analysis indicates that three of the four proteins responsible for the conversion of pantothenate (Pan) to CoASH in Escherichia coli are conserved in B. anthracis. In contrast, a novel type III pantothenate kinase (PanK) catalyzes the first committed step in the biosynthetic pathway in B. anthracis; unlike the E. coli type I PanK, this enzyme is not subject to feedback inhibition by CoASH. The crystal structure of B. anthracis PanK (BaPanK), solved using multiwavelength anomalous dispersion data and refined at a resolution of 2.0 A, demonstrates that BaPanK is a new member of the Acetate and Sugar Kinase/Hsc70/Actin (ASKHA) superfamily. The Pan and ATP substrates have been modeled into the active-site cleft; in addition to providing a clear rationale for the absence of CoASH inhibition, analysis of the Pan-binding pocket has led to the development of two new structure-based motifs (the PAN and INTERFACE motifs). Our analyses also suggest that the type III PanK in the spore-forming B. anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen.
| | [[Category: Bacillus anthracis str. Ames]] |
| | | [[Category: Large Structures]] |
| ==About this Structure==
| | [[Category: Nicely NI]] |
| 2H3G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H3G OCA].
| |
| | |
| ==Reference==
| |
| Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: implications for coenzyme A-dependent redox biology., Nicely NI, Parsonage D, Paige C, Newton GL, Fahey RC, Leonardi R, Jackowski S, Mallett TC, Claiborne A, Biochemistry. 2007 Mar 20;46(11):3234-45. Epub 2007 Feb 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17323930 17323930]
| |
| [[Category: Bacillus anthracis]] | |
| [[Category: Single protein]] | |
| [[Category: Nicely, N I.]] | |
| [[Category: anthrax]]
| |
| [[Category: askha]]
| |
| [[Category: bacillus anthracis]]
| |
| [[Category: coaa]]
| |
| [[Category: coax]]
| |
| [[Category: pantothenate kinase]]
| |
| [[Category: type iii pantothenate kinase]]
| |
| | |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:53 2008''
| |
