2cfb

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|PDB= 2cfb |SIZE=350|CAPTION= <scene name='initialview01'>2cfb</scene>, resolution 2.85&Aring;
|PDB= 2cfb |SIZE=350|CAPTION= <scene name='initialview01'>2cfb</scene>, resolution 2.85&Aring;
|SITE= <scene name='pdbsite=AC1:Plr+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Plr+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE'>PLR</scene>
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|LIGAND= <scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate-1-semialdehyde_2,1-aminomutase Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.8 5.4.3.8]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate-1-semialdehyde_2,1-aminomutase Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.8 5.4.3.8] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfb OCA], [http://www.ebi.ac.uk/pdbsum/2cfb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cfb RCSB]</span>
}}
}}
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[[Category: Schubert, W D.]]
[[Category: Schubert, W D.]]
[[Category: Schulze, J O.]]
[[Category: Schulze, J O.]]
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[[Category: PLR]]
 
[[Category: aminotransferase]]
[[Category: aminotransferase]]
[[Category: chlorophyll biosynthesis]]
[[Category: chlorophyll biosynthesis]]
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[[Category: tetrapyrrole biosynthesis]]
[[Category: tetrapyrrole biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:14:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:20:37 2008''

Revision as of 23:20, 30 March 2008

Image:2cfb.gif


PDB ID 2cfb

Drag the structure with the mouse to rotate
, resolution 2.85Å
Sites:
Ligands:
Activity: Glutamate-1-semialdehyde 2,1-aminomutase, with EC number 5.4.3.8
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE FROM THERMOSYNECHOCOCCUS ELONGATUS


Overview

Glutamate-1-semialdehyde 2,1-aminomutase (GSAM) is the second enzyme in the C(5) pathway of tetrapyrrole biosynthesis found in most bacteria, in archaea and in plants. It catalyzes the transamination of glutamate-1-semialdehyde to 5-aminolevulinic acid (ALA) in a pyridoxal 5'-phosphate (PLP)-dependent manner. We present the crystal structure of GSAM from the thermophilic cyanobacterium Thermosynechococcus elongatus (GSAM(Tel)) in its PLP-bound form at 2.85A resolution. GSAM(Tel) is a symmetric homodimer, whereas GSAM from Synechococcus (GSAM(Syn)) has been described as asymmetric. The symmetry of GSAM(Tel) thus challenges the previously proposed negative cooperativity between monomers of this enzyme. Furthermore, GSAM(Tel) reveals an extensive flexible region at the interface of the proposed complex of GSAM with glutamyl-tRNA reductase (GluTR), the preceding enzyme in tetrapyrrole biosynthesis. Compared to GSAM(Syn), the monomers of GSAM(Tel) are rotated away from each other along the dimerization interface by 10 degrees . The associated flexibility of GSAM may be essential for complex formation with GluTR to occur. Unexpectedly, we find that GSAM is structurally related to 5-aminolevulinate synthase (ALAS), the ALA-producing enzyme in the Shemin pathway of alpha-proteobacteria and non-plant eukaryotes. This structural relationship applies also to the corresponding subfamilies of PLP-dependent enzymes. We thus propose that the CoA-subfamily (including ALAS) and the aminotransferase subfamily II (including GSAM) are evolutionarily closely related and that ALAS may thus have evolved from GSAM.

About this Structure

2CFB is a Single protein structure of sequence from Synechococcus elongatus. Full crystallographic information is available from OCA.

Reference

Evolutionary relationship between initial enzymes of tetrapyrrole biosynthesis., Schulze JO, Schubert WD, Moser J, Jahn D, Heinz DW, J Mol Biol. 2006 May 19;358(5):1212-20. Epub 2006 Mar 10. PMID:16564539

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