2w5w
From Proteopedia
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| - | [[Image:2w5w.png|left|200px]] | ||
| - | + | ==Structure of TAB5 alkaline phosphatase mutant His 135 Asp with Zn bound in the M3 site.== | |
| + | <StructureSection load='2w5w' size='340' side='right'caption='[[2w5w]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2w5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Antarctic_bacterium_tab5 Antarctic bacterium tab5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W5W FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iuc|2iuc]], [[2w5v|2w5v]], [[2w5x|2w5x]]</div></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] </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=2w5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w5w OCA], [https://pdbe.org/2w5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w5w RCSB], [https://www.ebi.ac.uk/pdbsum/2w5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w5w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/w5/2w5w_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=2w5w ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Alkaline phosphatases (APs) are commercially applied enzymes that catalyze the hydrolysis of phosphate monoesters by a reaction involving three active site metal ions. We have previously identified H135 as the key residue for controlling activity of the psychrophilic TAB5 AP (TAP). In this paper we describe three X-ray crystallographic structures on TAP variants H135E and H135D in complex with a variety of metal ions. The structural analysis is supported by thermodynamic and kinetic data. The AP catalysis essentially requires octahedral coordination in the M3 site, but stability is adjusted with the conformational freedom of the metal ion. Comparison to the mesophilic E. coli alkaline phosphatase shows differences in the charge transfer network in providing the chemically optimal metal combination for catalysis. Our results provide explanation why the TAB5 and E. coli APs respond in an opposite way to mutagenesis in their active sites. They provide a lesson on chemical fine tuning and the importance of the second coordination sphere in defining metal specificity in enzymes. Understanding the framework of alkaline phosphatase catalysis is essential in the efforts to design even more powerful tools for modern biotechnology. | ||
| - | + | Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases.,Koutsioulis D, Lyskowski A, Maki S, Guthrie E, Feller G, Bouriotis V, Heikinheimo P Protein Sci. 2009 Nov 13. PMID:19916164<ref>PMID:19916164</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2w5w" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Alkaline phosphatase|Alkaline phosphatase]] | + | *[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]] |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
[[Category: Alkaline phosphatase]] | [[Category: Alkaline phosphatase]] | ||
[[Category: Antarctic bacterium tab5]] | [[Category: Antarctic bacterium tab5]] | ||
| - | [[Category: Bouriotis, V | + | [[Category: Large Structures]] |
| - | [[Category: Feller, G | + | [[Category: Bouriotis, V]] |
| - | [[Category: Guthrie, E | + | [[Category: Feller, G]] |
| - | [[Category: Heikinheimo, P | + | [[Category: Guthrie, E]] |
| - | [[Category: Koutsioulis, D | + | [[Category: Heikinheimo, P]] |
| - | [[Category: Lyskowski, A | + | [[Category: Koutsioulis, D]] |
| - | [[Category: Maki, S | + | [[Category: Lyskowski, A]] |
| - | + | [[Category: Maki, S]] | |
[[Category: Cold adaptation]] | [[Category: Cold adaptation]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Psychrophile]] | [[Category: Psychrophile]] | ||
Current revision
Structure of TAB5 alkaline phosphatase mutant His 135 Asp with Zn bound in the M3 site.
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