1n8p: Difference between revisions

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Crystal Structure of cystathionine gamma-lyase from yeast

OverviewOverview

The crystal structure of cystathionine gamma-lyase (CGL) from yeast has been solved by molecular replacement at a resolution of 2.6 A. The molecule consists of 393 amino acid residues and one PLP moiety and is arranged in the crystal as a tetramer with D2 symmetry as in other related enzymes of the Cys-Met-metabolism PLP-dependent family like cystathionine beta-lyase (CBL). A structure comparison with other family members revealed surprising insights into the tuning of enzymatic specificity between the different family members. CGLs from yeast or human are virtually identical at their active sites to cystathionine gamma-synthase (CGS) from E. coli. Both CGLs and bacterial CGSs exhibit gamma-synthase and gamma-lyase activities depending on their position in the metabolic pathway and the available substrates. This group of enzymes has a glutamate (E333 in yeast CGL) which binds to the distal group of cystathionine (CTT) or the amino group of cysteine. Plant CGSs use homoserine phosphate instead of O-succinyl-homoserine as one substrate. This is reflected by a partially different active site structure in plant CGSs. In CGL and CBL the pseudosymmetric substrate must dock at the active site in different orientations, with S in gamma-position (CBL) or in delta-position (CGL). The conserved glutamate steers the substrate as seen in other CGLs. In CBLs this position is occupied by either tyrosine or hydrophobic residues directing binding of CTT such that S is in the in gamma-position. In methionine gamma-lyase a hydrophic patch operates as recognition site for the methyl group of the methionine substrate.

About this StructureAbout this Structure

1N8P is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Cystathionine gamma-lyase, with EC number 4.4.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison., Messerschmidt A, Worbs M, Steegborn C, Wahl MC, Huber R, Laber B, Clausen T, Biol Chem. 2003 Mar;384(3):373-86. PMID:12715888

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 caption="1n8p, resolution 2.60&Aring;" />
 '''Crystal Structure of cystathionine gamma-lyase from yeast'''<br />
 ==Overview==
-The crystal structure of cystathionine gamma-lyase (CGL) from yeast has, been solved by molecular replacement at a resolution of 2.6 A. The, molecule consists of 393 amino acid residues and one PLP moiety and is, arranged in the crystal as a tetramer with D2 symmetry as in other related, enzymes of the Cys-Met-metabolism PLP-dependent family like cystathionine, beta-lyase (CBL). A structure comparison with other family members, revealed surprising insights into the tuning of enzymatic specificity, between the different family members. CGLs from yeast or human are, virtually identical at their active sites to cystathionine gamma-synthase, (CGS) from E. coli. Both CGLs and bacterial CGSs exhibit gamma-synthase, and gamma-lyase activities depending on their position in the metabolic, pathway and the available substrates. This group of enzymes has a, glutamate (E333 in yeast CGL) which binds to the distal group of, cystathionine (CTT) or the amino group of cysteine. Plant CGSs use, homoserine phosphate instead of O-succinyl-homoserine as one substrate., This is reflected by a partially different active site structure in plant, CGSs. In CGL and CBL the pseudosymmetric substrate must dock at the active, site in different orientations, with S in gamma-position (CBL) or in, delta-position (CGL). The conserved glutamate steers the substrate as seen, in other CGLs. In CBLs this position is occupied by either tyrosine or, hydrophobic residues directing binding of CTT such that S is in the in, gamma-position. In methionine gamma-lyase a hydrophic patch operates as, recognition site for the methyl group of the methionine substrate.
+The crystal structure of cystathionine gamma-lyase (CGL) from yeast has been solved by molecular replacement at a resolution of 2.6 A. The molecule consists of 393 amino acid residues and one PLP moiety and is arranged in the crystal as a tetramer with D2 symmetry as in other related enzymes of the Cys-Met-metabolism PLP-dependent family like cystathionine beta-lyase (CBL). A structure comparison with other family members revealed surprising insights into the tuning of enzymatic specificity between the different family members. CGLs from yeast or human are virtually identical at their active sites to cystathionine gamma-synthase (CGS) from E. coli. Both CGLs and bacterial CGSs exhibit gamma-synthase and gamma-lyase activities depending on their position in the metabolic pathway and the available substrates. This group of enzymes has a glutamate (E333 in yeast CGL) which binds to the distal group of cystathionine (CTT) or the amino group of cysteine. Plant CGSs use homoserine phosphate instead of O-succinyl-homoserine as one substrate. This is reflected by a partially different active site structure in plant CGSs. In CGL and CBL the pseudosymmetric substrate must dock at the active site in different orientations, with S in gamma-position (CBL) or in delta-position (CGL). The conserved glutamate steers the substrate as seen in other CGLs. In CBLs this position is occupied by either tyrosine or hydrophobic residues directing binding of CTT such that S is in the in gamma-position. In methionine gamma-lyase a hydrophic patch operates as recognition site for the methyl group of the methionine substrate.
 ==About this Structure==
-N8P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cystathionine_gamma-lyase Cystathionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.1 4.4.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N8P OCA].
+N8P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cystathionine_gamma-lyase Cystathionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.1 4.4.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8P OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: Messerschmidt, A.]]
 [[Category: Steegborn, C.]]
-[[Category: Wahl, M.C.]]
+[[Category: Wahl, M C.]]
 [[Category: Worbs, M.]]
 [[Category: PLP]]
 [[Category: three open alpha/beta structures]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:03:10 2007''
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