2bwo: Difference between revisions
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|PDB= 2bwo |SIZE=350|CAPTION= <scene name='initialview01'>2bwo</scene>, resolution 2.80Å | |PDB= 2bwo |SIZE=350|CAPTION= <scene name='initialview01'>2bwo</scene>, resolution 2.80Å | ||
|SITE= <scene name='pdbsite=AC1:Sca+Binding+Site+For+Chain+E'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Sca+Binding+Site+For+Chain+E'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SCA:SUCCINYL-COENZYME+A'>SCA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/5-aminolevulinate_synthase 5-aminolevulinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.37 2.3.1.37] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/5-aminolevulinate_synthase 5-aminolevulinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.37 2.3.1.37] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bwo OCA], [http://www.ebi.ac.uk/pdbsum/2bwo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bwo RCSB]</span> | |||
}} | }} | ||
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[[Category: Schubert, W D.]] | [[Category: Schubert, W D.]] | ||
[[Category: Schulze, J O.]] | [[Category: Schulze, J O.]] | ||
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
[[Category: heme biosynthesis]] | [[Category: heme biosynthesis]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:12:54 2008'' | ||
Revision as of 02:12, 31 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | 5-aminolevulinate synthase, with EC number 2.3.1.37 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
5-AMINOLEVULINATE SYNTHASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH SUCCINYL-COA
OverviewOverview
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 StructureAbout this Structure
2BWO is a Single protein structure of sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA.
ReferenceReference
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
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