1evj: Difference between revisions

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New page: left|200px<br /><applet load="1evj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1evj, resolution 2.70Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1evj.gif|left|200px]]<br /><applet load="1evj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1evj, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D'''<br />


==Overview==
==CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D==
N-terminal or C-terminal arms that extend from folded protein domains can, play a critical role in quaternary structure and other intermolecular, associations and/or in controlling biological activity. We have tested the, role of an extended N-terminal arm in the structure and function of a, periplasmic enzyme glucose-fructose oxidoreductase (GFOR) from Zymomonas, mobilis. We have determined the crystal structure of the NAD(+) complex of, a truncated form of the enzyme, GFORDelta, in which the first 22 residues, of the N-terminal arm of the mature protein have been deleted. The, structure, refined at 2.7 A resolution (R(cryst)=24.1%, R(free)=28.4%), shows that the truncated form of the enzyme forms a dimer and implies that, the N-terminal arm is essential for tetramer formation by wild-type GFOR., Truncation of the N-terminal arm also greatly increases the solvent, exposure of the cofactor; since GFOR activity is dependent on retention of, the cofactor during the catalytic cycle we conclude that the absence of, GFOR activity in this mutant results from dissociation of the cofactor., The N-terminal arm thus determines the quaternary structure and the, retention of the cofactor for GFOR activity and during translocation into, the periplasm. The structure of GFORDelta also shows how an additional, mutation, Ser64Asp, converts the strict NADP(+) specificity of wild-type, GFOR to a dual NADP(+)/NAD(+) specificity.
<StructureSection load='1evj' size='340' side='right'caption='[[1evj]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1evj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EVJ 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=1evj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1evj OCA], [https://pdbe.org/1evj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1evj RCSB], [https://www.ebi.ac.uk/pdbsum/1evj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1evj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GFO_ZYMMO GFO_ZYMMO]
== 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/ev/1evj_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=1evj ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EVJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EVJ OCA].
*[[Glucose-fructose oxidoreductase|Glucose-fructose oxidoreductase]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation., Lott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA, Baker EN, J Mol Biol. 2000 Dec 8;304(4):575-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11099381 11099381]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Zymomonas mobilis]]
[[Category: Zymomonas mobilis]]
[[Category: Baker, E.N.]]
[[Category: Baker EN]]
[[Category: Baker, H.M.]]
[[Category: Baker HM]]
[[Category: Halbig, D.]]
[[Category: Halbig D]]
[[Category: Hardman, M.J.]]
[[Category: Hardman MJ]]
[[Category: Lott, J.S.]]
[[Category: Lott JS]]
[[Category: Sprenger, G.A.]]
[[Category: Sprenger GA]]
[[Category: NAD]]
[[Category: n-terminal arm]]
[[Category: nadp/nad binding]]
[[Category: oligomerization state]]
[[Category: osmotic protection]]
[[Category: periplasm]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:21:22 2007''

Latest revision as of 10:07, 7 February 2024

CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64DCRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D

Structural highlights

1evj is a 4 chain structure with sequence from Zymomonas mobilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GFO_ZYMMO

Evolutionary Conservation

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

See Also

1evj, resolution 2.70Å

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