1m6s
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1m6s.jpg|left|200px]] | + | [[Image:1m6s.jpg|left|200px]] |
- | + | ||
- | '''Crystal Structure Of Threonine Aldolase''' | + | {{Structure |
+ | |PDB= 1m6s |SIZE=350|CAPTION= <scene name='initialview01'>1m6s</scene>, resolution 1.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</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= | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure Of Threonine Aldolase''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 1M6S is a [ | + | 1M6S 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=1M6S 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]] | ||
Line 24: | Line 33: | ||
[[Category: vitamin b12]] | [[Category: vitamin b12]] | ||
- | ''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 12:39:41 2008'' |
Revision as of 10:39, 20 March 2008
| |||||||
, resolution 1.8Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | and | ||||||
Activity: | Threonine aldolase, with EC number 4.1.2.5 | ||||||
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
Page seeded by OCA on Thu Mar 20 12:39:41 2008
Categories: Single protein | Thermotoga maritima | Threonine aldolase | Burley, S K. | Kielkopf, C L. | CA | CL | Enzyme | Plp | Pyridoxal phosphate | Threonine | Vitamin b12