1m6s

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(New page: 200px<br /><applet load="1m6s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6s, resolution 1.8&Aring;" /> '''Crystal Structure Of ...)
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caption="1m6s, resolution 1.8&Aring;" />
'''Crystal Structure Of Threonine Aldolase'''<br />
'''Crystal Structure Of Threonine Aldolase'''<br />
==Overview==
==Overview==
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L-Threonine acetaldehyde-lyase (threonine aldolase, TA) is a, pyridoxal-5'-phosphate-dependent (PLP) enzyme that catalyzes conversion of, L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary, glycine biosynthetic pathway. X-ray structures of Thermatoga maritima TA, have been determined as the apo-enzyme at 1.8 A resolution and bound to, substrate L-allo-threonine and product glycine at 1.9 and 2.0 A, resolution, respectively. Despite low pairwise sequence identities, TA is, a member of aspartate aminotransferase (AATase) fold family of PLP, enzymes. The enzyme forms a 222 homotetramer with the PLP cofactor bound, via a Schiff-base linkage to Lys199 within a domain interface. The, structure reveals bound calcium and chloride ions that appear to, contribute to catalysis and oligomerization, respectively. Although, L-threonine and L-allo-threonine are substrates for T. maritima TA, enzymatic assays revealed a strong preference for L-allo-threonine., Structures of the external aldimines with substrate/product reveal a pair, of histidines that may provide flexibility in substrate recognition., Variation in the threonine binding pocket may explain preferences for, L-allo-threonine versus L-threonine among TA family members.
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L-Threonine acetaldehyde-lyase (threonine aldolase, TA) is a pyridoxal-5'-phosphate-dependent (PLP) enzyme that catalyzes conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway. X-ray structures of Thermatoga maritima TA have been determined as the apo-enzyme at 1.8 A resolution and bound to substrate L-allo-threonine and product glycine at 1.9 and 2.0 A resolution, respectively. Despite low pairwise sequence identities, TA is a member of aspartate aminotransferase (AATase) fold family of PLP enzymes. The enzyme forms a 222 homotetramer with the PLP cofactor bound via a Schiff-base linkage to Lys199 within a domain interface. The structure reveals bound calcium and chloride ions that appear to contribute to catalysis and oligomerization, respectively. Although L-threonine and L-allo-threonine are substrates for T. maritima TA, enzymatic assays revealed a strong preference for L-allo-threonine. Structures of the external aldimines with substrate/product reveal a pair of histidines that may provide flexibility in substrate recognition. Variation in the threonine binding pocket may explain preferences for L-allo-threonine versus L-threonine among TA family members.
==About this Structure==
==About this Structure==
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1M6S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Threonine_aldolase Threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.5 4.1.2.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6S OCA].
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1M6S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Threonine_aldolase Threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.5 4.1.2.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6S OCA].
==Reference==
==Reference==
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Threonine aldolase]]
[[Category: Threonine aldolase]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
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[[Category: Kielkopf, C.L.]]
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[[Category: Kielkopf, C L.]]
[[Category: CA]]
[[Category: CA]]
[[Category: CL]]
[[Category: CL]]
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[[Category: vitamin b12]]
[[Category: vitamin b12]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:53:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:07 2008''

Revision as of 11:52, 21 February 2008


1m6s, resolution 1.8Å

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Crystal Structure Of Threonine Aldolase

Overview

L-Threonine acetaldehyde-lyase (threonine aldolase, TA) is a pyridoxal-5'-phosphate-dependent (PLP) enzyme that catalyzes conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway. X-ray structures of Thermatoga maritima TA have been determined as the apo-enzyme at 1.8 A resolution and bound to substrate L-allo-threonine and product glycine at 1.9 and 2.0 A resolution, respectively. Despite low pairwise sequence identities, TA is a member of aspartate aminotransferase (AATase) fold family of PLP enzymes. The enzyme forms a 222 homotetramer with the PLP cofactor bound via a Schiff-base linkage to Lys199 within a domain interface. The structure reveals bound calcium and chloride ions that appear to contribute to catalysis and oligomerization, respectively. Although L-threonine and L-allo-threonine are substrates for T. maritima TA, enzymatic assays revealed a strong preference for L-allo-threonine. Structures of the external aldimines with substrate/product reveal a pair of histidines that may provide flexibility in substrate recognition. Variation in the threonine binding pocket may explain preferences for L-allo-threonine versus L-threonine among TA family members.

About this Structure

1M6S is a Single protein structure of sequence from Thermotoga maritima with and as ligands. Active as Threonine aldolase, with EC number 4.1.2.5 Full crystallographic information is available from OCA.

Reference

X-ray structures of threonine aldolase complexes: structural basis of substrate recognition., Kielkopf CL, Burley SK, Biochemistry. 2002 Oct 1;41(39):11711-20. PMID:12269813

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