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{{STRUCTURE_1s80| PDB=1s80 | SCENE= }} | |||
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'''Structure of Serine Acetyltranferase from Haemophilis influenzae Rd''' | '''Structure of Serine Acetyltranferase from Haemophilis influenzae Rd''' | ||
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | ||
[[Category: Shapiro, L.]] | [[Category: Shapiro, L.]] | ||
[[Category: | [[Category: Left-handed parallel beta-helix]] | ||
[[Category: | [[Category: New york structural genomix research consortium]] | ||
[[Category: | [[Category: Nysgxrc]] | ||
[[Category: | [[Category: Protein structure initiative]] | ||
[[Category: | [[Category: Psi]] | ||
[[Category: | [[Category: Serine acetyltransferase]] | ||
[[Category: | [[Category: Structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:24:48 2008'' | |||
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Revision as of 05:24, 3 May 2008
Structure of Serine Acetyltranferase from Haemophilis influenzae Rd
Overview
The crystal structure of serine acetyltransferase (SAT) from Haemophilus influenzae Rd determined at 2.7 A resolution is presented. SAT is a member of a family of hexapeptide-containing transferases that contain six-residue tandem repeats (LIV)-G-X(4) that have been shown to form left-handed parallel beta-helices. In the current structure, each protomer is comprised of two domains: an N-terminal alpha-helical domain and a C-terminal left-handed parallel beta-helix domain. Although other members of this protein family are known to form trimeric structures, SAT forms a dimer of trimers in which the trimer interface is mediated through interactions between both the beta-helix domains and N-terminal domains; these trimers dimerize through contacts in the N-terminal domain. All dimer-of-trimer interactions are mediated through amino acids within an N-terminal extension common only to a subset of SATs, suggesting that members of this subfamily may also adopt hexameric structures. Putative active sites are formed by crevices between adjacent protomers in a trimer. Thus, six independent active sites exist in the hexameric enzyme complex.
About this Structure
1S80 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Structure of serine acetyltransferase from Haemophilus influenzae Rd., Gorman J, Shapiro L, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1600-5. Epub 2004, Aug 26. PMID:15333931 Page seeded by OCA on Sat May 3 08:24:48 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Haemophilus influenzae
- Serine O-acetyltransferase
- Single protein
- Burley, S K.
- Gogos, A.
- Gorman, J.
- NYSGXRC, New York Structural GenomiX Research Consortium.
- Shapiro, L.
- Left-handed parallel beta-helix
- New york structural genomix research consortium
- Nysgxrc
- Protein structure initiative
- Psi
- Serine acetyltransferase
- Structural genomic
