1dko: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1dko" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dko, resolution 2.380Å" /> '''CRYSTAL STRUCTURE O...
 
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1dko.gif|left|200px]]<br /><applet load="1dko" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dko, resolution 2.380&Aring;" />
'''CRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE==
Phytases catalyze the hydrolysis of phytate and are able to improve the, nutritional quality of phytate-rich diets. Escherichia coli phytase, a, member of the histidine acid phosphatase family has the highest specific, activity of all phytases characterized. The crystal structure of E. coli, phytase has been determined by a two-wavelength anomalous diffraction, method using the exceptionally strong anomalous scattering of tungsten., Despite a lack of sequence similarity, the structure closely resembles the, overall fold of other histidine acid phosphatases. The structure of E., coli phytase in complex with phytate, the preferred substrate, reveals the, binding mode and substrate recognition. The binding is also accompanied by, conformational changes which suggest that substrate binding enhances, catalysis by increasing the acidity of the general acid.
<StructureSection load='1dko' size='340' side='right'caption='[[1dko]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dko]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DKO 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]] 2.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</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=1dko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dko OCA], [https://pdbe.org/1dko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dko RCSB], [https://www.ebi.ac.uk/pdbsum/1dko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dko ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPA_ECOLI PPA_ECOLI]
== 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/dk/1dko_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=1dko ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1DKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with HG and WO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DKO OCA].
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
 
*[[Phytase 3D structures|Phytase 3D structures]]
==Reference==
__TOC__
Crystal structures of Escherichia coli phytase and its complex with phytate., Lim D, Golovan S, Forsberg CW, Jia Z, Nat Struct Biol. 2000 Feb;7(2):108-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10655611 10655611]
</StructureSection>
[[Category: Acid phosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Forsberg, C.W.]]
[[Category: Forsberg CW]]
[[Category: Golovan, S.]]
[[Category: Golovan S]]
[[Category: Jia, Z.]]
[[Category: Jia Z]]
[[Category: Lim, D.]]
[[Category: Lim D]]
[[Category: HG]]
[[Category: WO4]]
[[Category: histidine acid phosphatase fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:21:58 2007''

Latest revision as of 12:51, 20 March 2024

CRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGECRYSTAL STRUCTURE OF TUNGSTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6 WITH TUNGSTATE BOUND AT THE ACTIVE SITE AND WITH HG2+ CATION ACTING AS AN INTERMOLECULAR BRIDGE

Structural highlights

1dko is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.38Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PPA_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1dko, resolution 2.38Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA