2bwp
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2bwp.gif|left|200px]] | [[Image:2bwp.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2bwp", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2bwp| PDB=2bwp | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''5-AMINOLEVULINATE SYNTHASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH GLYCINE''' | '''5-AMINOLEVULINATE SYNTHASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH GLYCINE''' | ||
| Line 32: | Line 29: | ||
[[Category: Schubert, W D.]] | [[Category: Schubert, W D.]] | ||
[[Category: Schulze, J O.]] | [[Category: Schulze, J O.]] | ||
| - | [[Category: | + | [[Category: Acyltransferase]] |
| - | [[Category: | + | [[Category: Heme biosynthesis]] |
| - | [[Category: | + | [[Category: Pyridoxal phosphate dependent]] |
| - | [[Category: | + | [[Category: Tetrapyrrole biosynthesis]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:54:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:54, 3 May 2008
5-AMINOLEVULINATE SYNTHASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH GLYCINE
Overview
5-Aminolevulinate synthase (ALAS) is the first and rate-limiting enzyme of heme biosynthesis in humans, animals, other non-plant eukaryotes, and alpha-proteobacteria. It catalyzes the synthesis of 5-aminolevulinic acid, the first common precursor of all tetrapyrroles, from glycine and succinyl-coenzyme A (sCoA) in a pyridoxal 5'-phosphate (PLP)-dependent manner. X-linked sideroblastic anemias (XLSAs), a group of severe disorders in humans characterized by inadequate formation of heme in erythroblast mitochondria, are caused by mutations in the gene for erythroid eALAS, one of two human genes for ALAS. We present the first crystal structure of homodimeric ALAS from Rhodobacter capsulatus (ALAS(Rc)) binding its cofactor PLP. We, furthermore, present structures of ALAS(Rc) in complex with the substrates glycine or sCoA. The sequence identity of ALAS from R. capsulatus and human eALAS is 49%. XLSA-causing mutations may thus be mapped, revealing the molecular basis of XLSA in humans. Mutations are found to obstruct substrate binding, disrupt the dimer interface, or hamper the correct folding. The structure of ALAS completes the structural analysis of enzymes in heme biosynthesis.
About this Structure
2BWP is a Single protein structure of sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA.
Reference
Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans., Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW, EMBO J. 2005 Sep 21;24(18):3166-77. Epub 2005 Aug 25. PMID:16121195 Page seeded by OCA on Sat May 3 20:54:27 2008
