2yeq
From Proteopedia
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- | [[Image:2yeq.jpg|left|200px]] | ||
- | < | + | ==Structure of PhoD== |
- | + | <StructureSection load='2yeq' size='340' side='right'caption='[[2yeq]], [[Resolution|resolution]] 1.93Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2yeq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YEQ FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</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'>[https://proteopedia.org/fgij/fg.htm?mol=2yeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yeq OCA], [https://pdbe.org/2yeq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yeq RCSB], [https://www.ebi.ac.uk/pdbsum/2yeq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yeq ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/PPBD_BACSU PPBD_BACSU] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The PhoD family of extracytoplasmic phosphodiesterases are amongst the most commonly occurring bacterial phosphatases. The exemplars for this family are the PhoD protein of Bacillus subtilis and the phospholipase D of Streptomyces chromofuscus. We present the crystal structure of B. subtilis PhoD. PhoD is most closely related to purple acid phosphatases (PAPs) with both types of enzyme containing a tyrosinate-ligated Fe3+ ion. However, the PhoD active site diverges from that found in PAPs and uses two Ca2+ ions instead of the single extra Fe2+, Mn2+, or Zn2+ ion present in PAPs. The PhoD crystals contain a phosphate molecule that co-ordinates all three active site metal ions and which is proposed to represent a product complex. A C-terminal helix lies over the active site and controls access to the catalytic centre. The structure of PhoD defines a new phosphatase active site architecture based on Fe3+ and Ca2+ ions. | ||
- | + | Crystal Structure of the Bacillus subtilis Phosphodiesterase PhoD Reveals an Iron and Calcium-Containing Active Site.,Rodriguez F, Lillington J, Johnson S, Timmel CR, Lea SM, Berks BC J Biol Chem. 2014 Sep 12. pii: jbc.M114.604892. PMID:25217636<ref>PMID:25217636</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2yeq" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]] |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
- | [[Category: Berks | + | [[Category: Large Structures]] |
- | [[Category: Johnson | + | [[Category: Berks B]] |
- | [[Category: Lea | + | [[Category: Johnson SJ]] |
- | [[Category: Lillington | + | [[Category: Lea SM]] |
- | [[Category: Rodriguez | + | [[Category: Lillington JED]] |
- | [[Category: Roversi | + | [[Category: Rodriguez F]] |
- | + | [[Category: Roversi P]] | |
- | + |
Current revision
Structure of PhoD
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