1lw4: Difference between revisions
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|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> | |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 | |RELATEDENTRY=[[1lw5|1LW5]], [[1m6s|1M6S]] | ||
|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.rcsb.org/pdb/explore.do?structureId=1lw4 RCSB]</span> | |||
}} | }} | ||
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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 Sun Mar 30 22:08:06 2008'' | ||
Revision as of 19:08, 30 March 2008
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| 1lw4, resolution 1.9Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CA, CL, LLP, MSE, PLP, TLP | ||||||||||||
| Activity: | Threonine aldolase, with EC number 4.1.2.5 | ||||||||||||
| Domains: | Beta_elim_lyase, GLY1 | ||||||||||||
| Related: | 1LW5, 1M6S
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| Resources: | FirstGlance, OCA, PDBsum, 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 Sun Mar 30 22:08:06 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
