2cfb
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 2CFB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]] with PLR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 2CFB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]] with PLR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CFB OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16564539 16564539] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16564539 16564539] | ||
| + | [[Category: Glutamate-1-semialdehyde 2,1-aminomutase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechococcus elongatus]] | [[Category: Synechococcus elongatus]] | ||
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[[Category: tetrapyrrole biosynthesis]] | [[Category: tetrapyrrole biosynthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:34:40 2007'' |
Revision as of 08:29, 30 October 2007
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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 ... [(full description)]
About this Structure
2CFB is a [Single protein] structure of sequence from [Synechococcus elongatus] with PLR as [ligand]. Active as [Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [5.4.3.8]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 10:34:40 2007
Categories: Glutamate-1-semialdehyde 2,1-aminomutase | Single protein | Synechococcus elongatus | Heinz, D.W. | Jahn, D. | Moser, J. | Schubert, W.D. | Schulze, J.O. | PLR | Aminotransferase | Chlorophyll biosynthesis | Isomerase | Porphyrin biosynthesis | Pyridoxal phosphate dependent | Tetrapyrrole biosynthesis
