2c3z: Difference between revisions
New page: left|200px<br /> <applet load="2c3z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c3z, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| Line 8: | Line 8: | ||
==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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.48 4.1.1.48]]. 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== | ||
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16342933 16342933] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16342933 16342933] | ||
[[Category: Indole-3-glycerol-phosphate synthase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
| Line 30: | Line 31: | ||
[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:11:15 2007'' | ||
Revision as of 13:06, 30 October 2007
|
CRYSTAL STRUCTURE OF A TRUNCATED VARIANT OF INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
2C3Z is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with SO4 as [ligand]. Active as [Indole-3-glycerol-phosphate synthase], with EC number [4.1.1.48]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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
Page seeded by OCA on Tue Oct 30 12:11:15 2007
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- 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