2c3z: Difference between revisions

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==Overview==
==Overview==
Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in, the biosynthesis of tryptophan. It belongs to the large and versatile, family of (betaalpha)(8)-barrel enzymes but has an unusual N-terminal, extension of about 40 residues. Limited proteolysis with trypsin of IGPS, from both Sulfolobus solfataricus (sIGPS) and Thermotoga maritima (tIGPS), removes about 25 N-terminal residues and one of the two extra helices, contained therein. To assess the role of the extension, the N-terminally, truncated variants sIGPSDelta(1-26) and tIGPSDelta(1-25) were produced, recombinantly in Escherichia coli, purified, and characterized in, comparison to the wild-type enzymes. Both sIGPSDelta(1-26) and, tIGPSDelta(1-25) have unchanged oligomerization states and turnover, numbers. In ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16342933 (full description)]]
Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in, the biosynthesis of tryptophan. It belongs to the large and versatile, family of (betaalpha)(8)-barrel enzymes but has an unusual N-terminal, extension of about 40 residues. Limited proteolysis with trypsin of IGPS, from both Sulfolobus solfataricus (sIGPS) and Thermotoga maritima (tIGPS), removes about 25 N-terminal residues and one of the two extra helices, contained therein. To assess the role of the extension, the N-terminally, truncated variants sIGPSDelta(1-26) and tIGPSDelta(1-25) were produced, recombinantly in Escherichia coli, purified, and characterized in, comparison to the wild-type enzymes. Both sIGPSDelta(1-26) and, tIGPSDelta(1-25) have unchanged oligomerization states and turnover, numbers. In contrast, their Michaelis constants for the substrate, 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate are increased, and, their resistance toward unfolding induced by heat and guanidinium chloride, is decreased. sIGPSDelta(1-26) was crystallized, and its X-ray structure, was solved at 2.8 A resolution. The comparison with the known structure of, sIGPS reveals small differences that account for its reduced substrate, affinity and protein stability. The structure of the core of, sIGPSDelta(1-26) is, however, unchanged compared to sIGPS, explaining its, retained catalytic activity and consistent with the idea that it evolved, from the same ancestor as the phosphoribosyl anthranilate isomerase and, the alpha-subunit of tryptophan synthase. These (betaalpha)(8)-barrel, enzymes catalyze the reactions preceding and following IGPS in tryptophan, biosynthesis but lack an N-terminal extension.


==About this Structure==
==About this Structure==
2C3Z is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Indole-3-glycerol-phosphate_synthase Indole-3-glycerol-phosphate synthase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.48 4.1.1.48]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3Z OCA]].  
2C3Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Indole-3-glycerol-phosphate_synthase Indole-3-glycerol-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.48 4.1.1.48] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3Z OCA].  


==Reference==
==Reference==
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[[Category: tryptophan biosynthesis]]
[[Category: tryptophan biosynthesis]]


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