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1lw4
From Proteopedia
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| - | [[Image:1lw4.gif|left|200px]] | + | [[Image:1lw4.gif|left|200px]] |
| - | + | ||
| - | '''X-ray structure of L-Threonine Aldolase (low-specificity) in complex with L-allo-threonine''' | + | {{Structure |
| + | |PDB= 1lw4 |SIZE=350|CAPTION= <scene name='initialview01'>1lw4</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TLP:3-HYDROXY-2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-BUTYRIC+ACID'>TLP</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-ray structure of L-Threonine Aldolase (low-specificity) in complex with L-allo-threonine''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LW4 is a [ | + | 1LW4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LW4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12269813 12269813] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: psi]] | [[Category: psi]] | ||
[[Category: pyridoxal-5-phosphate]] | [[Category: pyridoxal-5-phosphate]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: threonine]] | [[Category: threonine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:56 2008'' |
Revision as of 10:35, 20 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Activity: | Threonine aldolase, with EC number 4.1.2.5 | ||||||
| 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 Thu Mar 20 12:35:56 2008
Categories: Single protein | Thermotoga maritima | Threonine aldolase | Burley, S K. | Kielkopf, C L. | NYSGXRC, New York Structural GenomiX Research Consortium. | CA | CL | PLP | TLP | Enzyme | New york structural genomix research consortium | Nysgxrc | Plp | Product complex | Protein structure initiative | Psi | Pyridoxal-5-phosphate | Structural genomic | Threonine
