1m6s
From Proteopedia
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|PDB= 1m6s |SIZE=350|CAPTION= <scene name='initialview01'>1m6s</scene>, resolution 1.8Å | |PDB= 1m6s |SIZE=350|CAPTION= <scene name='initialview01'>1m6s</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lw4|1LW4]], [[1lw5|1LW5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6s OCA], [http://www.ebi.ac.uk/pdbsum/1m6s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m6s RCSB]</span> | ||
}} | }} | ||
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[[Category: Burley, S K.]] | [[Category: Burley, S K.]] | ||
[[Category: Kielkopf, C L.]] | [[Category: Kielkopf, C L.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
[[Category: plp]] | [[Category: plp]] | ||
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[[Category: vitamin b12]] | [[Category: vitamin b12]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:06 2008'' |
Revision as of 19:12, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Threonine aldolase, with EC number 4.1.2.5 | ||||||
| Related: | 1LW4, 1LW5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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