1flj: Difference between revisions

Revision as of 13:40, 21 February 2008

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

OverviewOverview

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.

About this StructureAbout this Structure

1FLJ is a Single protein structure of sequence from Rattus norvegicus with , and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.

ReferenceReference

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:11024467

Page seeded by OCA on Thu Feb 21 12:39:53 2008

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

OCA

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-[[Image:1flj.jpg|left|200px]]<br /><applet load="1flj" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1flj.jpg|left|200px]]<br /><applet load="1flj" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1flj, resolution 1.80&Aring;" />
 '''CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-FLJ 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].
+FLJ 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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=GTT:'>GTT</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLJ OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Chatterjee, T.K.]]
+[[Category: Chatterjee, T K.]]
 [[Category: Darmawan, S.]]
-[[Category: Fisher, R.A.]]
+[[Category: Fisher, R A.]]
-[[Category: Honzatko, R.B.]]
+[[Category: Honzatko, R B.]]
-[[Category: Mallis, R.J.]]
+[[Category: Mallis, R J.]]
-[[Category: Poland, B.W.]]
+[[Category: Poland, B W.]]
-[[Category: Thomas, J.A.]]
+[[Category: Thomas, J A.]]
 [[Category: ACE]]
 [[Category: GTT]]
@@ Line 29: / Line 29: @@
 [[Category: s-glutathionylated]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:01:12 2007''
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