2ajt: Difference between revisions

Revision as of 17:28, 21 February 2008

Crystal structure of L-Arabinose Isomerase from E.coli

OverviewOverview

Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of commercial interest as it catalyzes the conversion of D-galactose to D-tagatose in vitro. The crystal structure of ECAI was solved and refined at 2.6 A resolution. The subunit structure of ECAI is organised into three domains: an N-terminal, a central and a C-terminal domain. It forms a crystallographic trimeric architecture in the asymmetric unit. Packing within the crystal suggests the idea that ECAI can form a hexameric assembly. Previous electron microscopic and biochemical studies supports that ECAI is hexameric in solution. A comparison with other known structures reveals that ECAI adopts a protein fold most similar to E. coli fucose isomerase (ECFI) despite very low sequence identity 9.7%. The structural similarity between ECAI and ECFI with regard to number of domains, overall fold, biological assembly, and active site architecture strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular determinants responsible for isomerization of arabinose to ribulose in vivo and galactose to tagatose in vitro.

About this StructureAbout this Structure

2AJT is a Single protein structure of sequence from Escherichia coli. Active as L-arabinose isomerase, with EC number 5.3.1.4 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production., Manjasetty BA, Chance MR, J Mol Biol. 2006 Jul 7;360(2):297-309. Epub 2006 May 5. PMID:16756997

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-[[Image:2ajt.gif|left|200px]]<br /><applet load="2ajt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2ajt.gif|left|200px]]<br /><applet load="2ajt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2ajt, resolution 2.60&Aring;" />
 '''Crystal structure of L-Arabinose Isomerase from E.coli'''<br />
 ==Overview==
-Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the, isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of, commercial interest as it catalyzes the conversion of D-galactose to, D-tagatose in vitro. The crystal structure of ECAI was solved and refined, at 2.6 A resolution. The subunit structure of ECAI is organised into three, domains: an N-terminal, a central and a C-terminal domain. It forms a, crystallographic trimeric architecture in the asymmetric unit. Packing, within the crystal suggests the idea that ECAI can form a hexameric, assembly. Previous electron microscopic and biochemical studies supports, that ECAI is hexameric in solution. A comparison with other known, structures reveals that ECAI adopts a protein fold most similar to E. coli, fucose isomerase (ECFI) despite very low sequence identity 9.7%. The, structural similarity between ECAI and ECFI with regard to number of, domains, overall fold, biological assembly, and active site architecture, strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular, determinants responsible for isomerization of arabinose to ribulose in, vivo and galactose to tagatose in vitro.
+Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of commercial interest as it catalyzes the conversion of D-galactose to D-tagatose in vitro. The crystal structure of ECAI was solved and refined at 2.6 A resolution. The subunit structure of ECAI is organised into three domains: an N-terminal, a central and a C-terminal domain. It forms a crystallographic trimeric architecture in the asymmetric unit. Packing within the crystal suggests the idea that ECAI can form a hexameric assembly. Previous electron microscopic and biochemical studies supports that ECAI is hexameric in solution. A comparison with other known structures reveals that ECAI adopts a protein fold most similar to E. coli fucose isomerase (ECFI) despite very low sequence identity 9.7%. The structural similarity between ECAI and ECFI with regard to number of domains, overall fold, biological assembly, and active site architecture strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular determinants responsible for isomerization of arabinose to ribulose in vivo and galactose to tagatose in vitro.
 ==About this Structure==
-AJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/L-arabinose_isomerase L-arabinose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.4 5.3.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AJT OCA].
+AJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/L-arabinose_isomerase L-arabinose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.4 5.3.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJT OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: L-arabinose isomerase]]
 [[Category: Single protein]]
-[[Category: Almo, S.C.]]
+[[Category: Almo, S C.]]
-[[Category: Burley, S.K.]]
+[[Category: Burley, S K.]]
-[[Category: Chance, M.R.]]
+[[Category: Chance, M R.]]
-[[Category: Fedorov, E.V.]]
+[[Category: Fedorov, E V.]]
-[[Category: Manjasetty, B.A.]]
+[[Category: Manjasetty, B A.]]
-[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
+[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
 [[Category: arabinose catabolism]]
 [[Category: carbohydrate metabolism]]
@@ Line 29: / Line 29: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:10:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:08 2008''