2c7t: Difference between revisions

Revision as of 17:45, 21 February 2008

CRYSTAL STRUCTURE OF THE PLP-BOUND FORM OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.

OverviewOverview

The aminotransferase (BtrR), which is involved in the biosynthesis of butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyses the pyridoxal phosphate (PLP)-dependent transamination reaction both of 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-DOS. The high-resolution crystal structures of the PLP- and PMP-bound forms of BtrR aminotransferase from B. circulans were solved at resolutions of 2.1 A and 1.7 A with R(factor)/R(free) values of 17.4/20.6 and 19.9/21.9, respectively. BtrR has a fold characteristic of the aspartate aminotransferase family, and sequence and structure analysis categorises it as a member of SMAT (secondary metabolite aminotransferases) subfamily. It exists as a homodimer with two active sites per dimer. The active site of the BtrR protomer is located in a cleft between an alpha helical N-terminus, a central alphabetaalpha sandwich domain and an alphabeta C-terminal domain. The structures of the PLP- and PMP-bound enzymes are very similar; however BtrR-PMP lacks the covalent bond to Lys192. Furthermore, the two forms differ in the side-chain conformations of Trp92, Asp163, and Tyr342 that are likely to be important in substrate selectivity and substrate binding. This is the first three-dimensional structure of an enzyme from the butirosin biosynthesis gene cluster.

About this StructureAbout this Structure

2C7T is a Single protein structure of sequence from Bacillus circulans with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis., Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB, Proteins. 2006 Oct 1;65(1):220-30. PMID:16894611

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 ==Overview==
-The aminotransferase (BtrR), which is involved in the biosynthesis of, butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside, antibiotic produced by Bacillus circulans, catalyses the pyridoxal, phosphate (PLP)-dependent transamination reaction both of, 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosamine and of, amino-dideoxy-scyllo-inosose to 2-DOS. The high-resolution crystal, structures of the PLP- and PMP-bound forms of BtrR aminotransferase from, B. circulans were solved at resolutions of 2.1 A and 1.7 A with, R(factor)/R(free) values of 17.4/20.6 and 19.9/21.9, respectively. BtrR, has a fold characteristic of the aspartate aminotransferase family, and, sequence and structure analysis categorises it as a member of SMAT, (secondary metabolite aminotransferases) subfamily. It exists as a, homodimer with two active sites per dimer. The active site of the BtrR, protomer is located in a cleft between an alpha helical N-terminus, a, central alphabetaalpha sandwich domain and an alphabeta C-terminal domain., The structures of the PLP- and PMP-bound enzymes are very similar; however, BtrR-PMP lacks the covalent bond to Lys192. Furthermore, the two forms, differ in the side-chain conformations of Trp92, Asp163, and Tyr342 that, are likely to be important in substrate selectivity and substrate binding., This is the first three-dimensional structure of an enzyme from the, butirosin biosynthesis gene cluster.
+The aminotransferase (BtrR), which is involved in the biosynthesis of butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyses the pyridoxal phosphate (PLP)-dependent transamination reaction both of 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-DOS. The high-resolution crystal structures of the PLP- and PMP-bound forms of BtrR aminotransferase from B. circulans were solved at resolutions of 2.1 A and 1.7 A with R(factor)/R(free) values of 17.4/20.6 and 19.9/21.9, respectively. BtrR has a fold characteristic of the aspartate aminotransferase family, and sequence and structure analysis categorises it as a member of SMAT (secondary metabolite aminotransferases) subfamily. It exists as a homodimer with two active sites per dimer. The active site of the BtrR protomer is located in a cleft between an alpha helical N-terminus, a central alphabetaalpha sandwich domain and an alphabeta C-terminal domain. The structures of the PLP- and PMP-bound enzymes are very similar; however BtrR-PMP lacks the covalent bond to Lys192. Furthermore, the two forms differ in the side-chain conformations of Trp92, Asp163, and Tyr342 that are likely to be important in substrate selectivity and substrate binding. This is the first three-dimensional structure of an enzyme from the butirosin biosynthesis gene cluster.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus circulans]]
 [[Category: Single protein]]
-[[Category: Blundell, T.L.]]
+[[Category: Blundell, T L.]]
-[[Category: Chirgadze, D.Y.]]
+[[Category: Chirgadze, D Y.]]
 [[Category: Huang, F.]]
 [[Category: Popovic, B.]]
-[[Category: Spencer, J.B.]]
+[[Category: Spencer, J B.]]
 [[Category: Tang, X.]]
 [[Category: PLP]]
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 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:32:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:51 2008''