1flj: Difference between revisions

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New page: left|200px<br /><applet load="1flj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1flj, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1flj.jpg|left|200px]]<br /><applet load="1flj" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III'''<br />


==Overview==
==CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III==
S-Glutathiolation of carbonic anhydrase III (CAIII) occurs rapidly in, hepatocytes under oxidative stress. The crystal structure of the, S-glutathiolated CAIII from rat liver reveals covalent adducts on, cysteines 183 and 188. Electrostatic charge and steric contacts at each, modification site inversely correlate with the relative rates of, reactivity of these cysteines toward glutathione (GSH). Diffuse electron, density associated with the GSH adducts suggests a lack of preferred, bonding interactions between CAIII and the glutathionyl moieties. Hence, the GSH adducts are available for binding by a protein capable of reducing, this mixed disulfide. These properties are consistent with the, participation of CAIII in the protection/recovery from the damaging, effects of oxidative agents.
<StructureSection load='1flj' size='340' side='right'caption='[[1flj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1flj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FLJ 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flj OCA], [https://pdbe.org/1flj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1flj RCSB], [https://www.ebi.ac.uk/pdbsum/1flj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1flj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAH3_RAT CAH3_RAT] Reversible hydration of carbon dioxide. A major participant in the liver response to oxidative stress.
== 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/fl/1flj_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=1flj ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FLJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN, ACE and GTT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FLJ OCA].
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of S-glutathiolated carbonic anhydrase III., Mallis RJ, Poland BW, Chatterjee TK, Fisher RA, Darmawan S, Honzatko RB, Thomas JA, FEBS Lett. 2000 Oct 6;482(3):237-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11024467 11024467]
[[Category: Large Structures]]
[[Category: Carbonate dehydratase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Chatterjee TK]]
[[Category: Chatterjee, T.K.]]
[[Category: Darmawan S]]
[[Category: Darmawan, S.]]
[[Category: Fisher RA]]
[[Category: Fisher, R.A.]]
[[Category: Honzatko RB]]
[[Category: Honzatko, R.B.]]
[[Category: Mallis RJ]]
[[Category: Mallis, R.J.]]
[[Category: Poland BW]]
[[Category: Poland, B.W.]]
[[Category: Thomas JA]]
[[Category: Thomas, J.A.]]
[[Category: ACE]]
[[Category: GTT]]
[[Category: ZN]]
[[Category: carbonic anhydrase iii]]
[[Category: glutathione]]
[[Category: s-glutathiolated]]
[[Category: s-glutathionylated]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:01:12 2007''

Latest revision as of 14:14, 27 March 2024

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE IIICRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

Structural highlights

1flj is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAH3_RAT Reversible hydration of carbon dioxide. A major participant in the liver response to oxidative stress.

Evolutionary Conservation

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

See Also

1flj, resolution 1.80Å

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