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.


4bhe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4bhe| PDB=4bhe | SCENE= }}
 +
===Methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP===
-
The entry 4bhe is ON HOLD until Paper Publication
+
==Function==
 +
[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>
-
Authors: Saccoccia, F., Angelucci, F., Ilari, A.
+
==About this Structure==
 +
[[4bhe]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHE OCA].
-
Description: Methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP
+
==Reference==
 +
<references group="xtra"/><references/>
 +
[[Category: Angelucci, F.]]
 +
[[Category: Ilari, A.]]
 +
[[Category: Saccoccia, F.]]
 +
[[Category: Transferase]]

Revision as of 09:58, 16 April 2014

Template:STRUCTURE 4bhe

Contents

Methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP

Function

[GLYA_METJA] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.[1]

About this Structure

4bhe is a 12 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Angelaccio S, Chiaraluce R, Consalvi V, Buchenau B, Giangiacomo L, Bossa F, Contestabile R. Catalytic and thermodynamic properties of tetrahydromethanopterin-dependent serine hydroxymethyltransferase from Methanococcus jannaschii. J Biol Chem. 2003 Oct 24;278(43):41789-97. Epub 2003 Aug 5. PMID:12902326 doi:http://dx.doi.org/10.1074/jbc.M306747200

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bhe"
Personal tools