2bwp

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[[Image:2bwp.gif|left|200px]]<br /><applet load="2bwp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bwp.gif|left|200px]]
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caption="2bwp, resolution 2.70&Aring;" />
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'''5-AMINOLEVULINATE SYNTHASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH GLYCINE'''<br />
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{{Structure
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|PDB= 2bwp |SIZE=350|CAPTION= <scene name='initialview01'>2bwp</scene>, resolution 2.70&Aring;
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|SITE= <scene name='pdbsite=AC1:Cbm+Binding+Site+For+Chain+E'>AC1</scene>
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|LIGAND= <scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|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]
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|GENE=
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}}
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'''5-AMINOLEVULINATE SYNTHASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH GLYCINE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BWP 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 <scene name='pdbligand=PLG:'>PLG</scene> and <scene name='pdbligand=ACY:'>ACY</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Cbm+Binding+Site+For+Chain+E'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWP OCA].
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2BWP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWP OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/16121195 16121195]
[[Category: 5-aminolevulinate synthase]]
[[Category: 5-aminolevulinate synthase]]
[[Category: Rhodobacter capsulatus]]
[[Category: Rhodobacter capsulatus]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:07:44 2008''

Revision as of 14:07, 20 March 2008

Image:2bwp.gif


PDB ID 2bwp

Drag the structure with the mouse to rotate
, resolution 2.70Å
Sites:
Ligands: and
Activity: 5-aminolevulinate synthase, with EC number 2.3.1.37
Coordinates: save as pdb, mmCIF, xml



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

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