2c3z: Difference between revisions
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[[Image:2c3z.gif|left|200px]] | [[Image:2c3z.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF A TRUNCATED VARIANT OF INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS''' | {{Structure | ||
|PDB= 2c3z |SIZE=350|CAPTION= <scene name='initialview01'>2c3z</scene>, resolution 2.8Å | |||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF A TRUNCATED VARIANT OF INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2C3Z is a [ | 2C3Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3Z OCA]. | ||
==Reference== | ==Reference== | ||
Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity., Schneider B, Knochel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R, Biochemistry. 2005 Dec 20;44(50):16405-12. PMID:[http:// | Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity., Schneider B, Knochel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R, Biochemistry. 2005 Dec 20;44(50):16405-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16342933 16342933] | ||
[[Category: Indole-3-glycerol-phosphate synthase]] | [[Category: Indole-3-glycerol-phosphate synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:10:30 2008'' | ||
Revision as of 14:10, 20 March 2008
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| 2c3z, resolution 2.8Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | SO4 | ||||||||||||
| Activity: | Indole-3-glycerol-phosphate synthase, with EC number 4.1.1.48 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF A TRUNCATED VARIANT OF INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS
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 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
2C3Z is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity., Schneider B, Knochel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R, Biochemistry. 2005 Dec 20;44(50):16405-12. PMID:16342933
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Indole-3-glycerol-phosphate synthase
- Single protein
- Sulfolobus solfataricus
- Darimont, B.
- Dietrich, S.
- Hennig, M.
- Kirschner, K.
- Knoechel, T.
- Schneider, A.
- Sterner, R.
- SO4
- Catalytic activity
- Decarboxylase
- Divergent evolution
- Indole-3-glycerol phosphate synthase
- Lyase
- Protein stability
- Tryptophan biosynthesis
