2bwo: Difference between revisions
New page: left|200px<br /> <applet load="2bwo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bwo, resolution 2.80Å" /> '''5-AMINOLEVULINATE S... |
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==About this Structure== | ==About this Structure== | ||
2BWO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]] with SCA and PLP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.37 2.3.1.37]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWO OCA]]. | 2BWO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]] with SCA and PLP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWO OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16121195 16121195] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16121195 16121195] | ||
[[Category: 5-aminolevulinate synthase]] | |||
[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 12:00, 30 October 2007
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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 ... [(full description)]
About this StructureAbout this Structure
2BWO is a [Single protein] structure of sequence from [Rhodobacter capsulatus] with SCA and PLP as [ligands]. Active as [5-aminolevulinate synthase], with EC number [2.3.1.37]. Structure known Active Site: AC1. 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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