This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1lw5
From Proteopedia
| Line 8: | Line 8: | ||
|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=1lw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lw5 OCA], [http://www.ebi.ac.uk/pdbsum/1lw5 PDBsum | + | |RELATEDENTRY=[[1lw4|1LW4]], [[1m6s|1M6S]] |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lw5 OCA], [http://www.ebi.ac.uk/pdbsum/1lw5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lw5 RCSB]</span> | ||
}} | }} | ||
| Line 39: | Line 40: | ||
[[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
| |||||||
| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Activity: | Threonine aldolase, with EC number 4.1.2.5 | ||||||
| Domains: | Beta_elim_lyase, GLY1 | ||||||
| Related: | 1LW4, 1M6S
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray structure of L-Threonine Aldolase (low-specificity) in complex with glycine
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
1LW5 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
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
