1lw4
From Proteopedia
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|PDB= 1lw4 |SIZE=350|CAPTION= <scene name='initialview01'>1lw4</scene>, resolution 1.9Å | |PDB= 1lw4 |SIZE=350|CAPTION= <scene name='initialview01'>1lw4</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | + | |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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=TLP:3-HYDROXY-2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-BUTYRIC+ACID'>TLP</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=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01212 Beta_elim_lyase], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG2008 GLY1]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lw4 OCA], [http://www.ebi.ac.uk/pdbsum/1lw4 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1lw4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kielkopf, C L.]] | [[Category: Kielkopf, C L.]] | ||
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: PLP]] | ||
| - | [[Category: TLP]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
[[Category: new york structural genomix research consortium]] | [[Category: new york structural genomix research consortium]] | ||
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[[Category: threonine]] | [[Category: threonine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:56:21 2008'' |
Revision as of 03:56, 26 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Activity: | Threonine aldolase, with EC number 4.1.2.5 | ||||||
| Domains: | Beta_elim_lyase, GLY1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray structure of L-Threonine Aldolase (low-specificity) in complex with L-allo-threonine
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
1LW4 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
Page seeded by OCA on Wed Mar 26 05:56:21 2008
Categories: Single protein | Thermotoga maritima | Threonine aldolase | Burley, S K. | Kielkopf, C L. | NYSGXRC, New York Structural GenomiX Research Consortium. | Enzyme | New york structural genomix research consortium | Nysgxrc | Plp | Product complex | Protein structure initiative | Psi | Pyridoxal-5-phosphate | Structural genomic | Threonine
