1s80
From Proteopedia
(New page: 200px<br /><applet load="1s80" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s80, resolution 2.70Å" /> '''Structure of Serine ...) |
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| - | [[Image:1s80.gif|left|200px]]<br /><applet load="1s80" size=" | + | [[Image:1s80.gif|left|200px]]<br /><applet load="1s80" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s80, resolution 2.70Å" /> | caption="1s80, resolution 2.70Å" /> | ||
'''Structure of Serine Acetyltranferase from Haemophilis influenzae Rd'''<br /> | '''Structure of Serine Acetyltranferase from Haemophilis influenzae Rd'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of serine acetyltransferase (SAT) from Haemophilus | + | 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== | ==About this Structure== | ||
| - | 1S80 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Serine_O-acetyltransferase Serine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.30 2.3.1.30] Full crystallographic information is available from [http:// | + | 1S80 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Serine_O-acetyltransferase Serine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.30 2.3.1.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S80 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Serine O-acetyltransferase]] | [[Category: Serine O-acetyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Gogos, A.]] | [[Category: Gogos, A.]] | ||
[[Category: Gorman, J.]] | [[Category: Gorman, J.]] | ||
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: Shapiro, L.]] | [[Category: Shapiro, L.]] | ||
[[Category: new york structural genomix research consortium]] | [[Category: new york structural genomix research consortium]] | ||
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[[Category: structural genomics; protein structure initiative; serine acetyltransferase; left-handed parallel beta-helix; nysgxrc]] | [[Category: structural genomics; protein structure initiative; serine acetyltransferase; left-handed parallel beta-helix; nysgxrc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:54 2008'' |
Revision as of 12:58, 21 February 2008
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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. Active as Serine O-acetyltransferase, with EC number 2.3.1.30 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 Thu Feb 21 14:58:54 2008
Categories: Haemophilus influenzae | Serine O-acetyltransferase | Single protein | Burley, S K. | Gogos, A. | Gorman, J. | NYSGXRC, New York Structural GenomiX Research Consortium. | Shapiro, L. | New york structural genomix research consortium | Nysgxrc | Psi | Structural genomics; protein structure initiative; serine acetyltransferase; left-handed parallel beta-helix; nysgxrc
