1lw4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1lw4.gif|left|200px]]
[[Image:1lw4.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1lw4 |SIZE=350|CAPTION= <scene name='initialview01'>1lw4</scene>, resolution 1.9&Aring;
+
The line below this paragraph, containing "STRUCTURE_1lw4", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|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&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=TLP:3-HYDROXY-2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-BUTYRIC+ACID'>TLP</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|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>
+
or leave the SCENE parameter empty for the default display.
-
|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>
+
{{STRUCTURE_1lw4| PDB=1lw4 | SCENE= }}
-
|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>
+
-
}}
+
'''X-ray structure of L-Threonine Aldolase (low-specificity) in complex with L-allo-threonine'''
'''X-ray structure of L-Threonine Aldolase (low-specificity) in complex with L-allo-threonine'''
Line 29: Line 26:
[[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: enzyme]]
+
[[Category: Enzyme]]
-
[[Category: new york structural genomix research consortium]]
+
[[Category: New york structural genomix research consortium]]
-
[[Category: nysgxrc]]
+
[[Category: Nysgxrc]]
-
[[Category: plp]]
+
[[Category: Plp]]
-
[[Category: product complex]]
+
[[Category: Product complex]]
-
[[Category: protein structure initiative]]
+
[[Category: Protein structure initiative]]
-
[[Category: psi]]
+
[[Category: Psi]]
-
[[Category: pyridoxal-5-phosphate]]
+
[[Category: Pyridoxal-5-phosphate]]
-
[[Category: structural genomic]]
+
[[Category: Structural genomic]]
-
[[Category: threonine]]
+
[[Category: Threonine]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:21:25 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:08:06 2008''
+

Revision as of 21:21, 2 May 2008

Image:1lw4.gif

Template:STRUCTURE 1lw4

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 Sat May 3 00:21:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lw4"
Personal tools