1gn0: Difference between revisions
New page: left|200px<br /><applet load="1gn0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gn0, resolution 1.8Å" /> '''ESCHERICHIA COLI GLPE... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1gn0.jpg|left|200px]]<br /><applet load="1gn0" size=" | [[Image:1gn0.jpg|left|200px]]<br /><applet load="1gn0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1gn0, resolution 1.8Å" /> | caption="1gn0, resolution 1.8Å" /> | ||
'''ESCHERICHIA COLI GLPE SULFURTRANSFERASE SOAKED WITH KCN'''<br /> | '''ESCHERICHIA COLI GLPE SULFURTRANSFERASE SOAKED WITH KCN'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: Rhodanese domains are structural modules occurring in the | BACKGROUND: Rhodanese domains are structural modules occurring in the three major evolutionary phyla. They are found as single-domain proteins, as tandemly repeated modules in which the C-terminal domain only bears the properly structured active site, or as members of multidomain proteins. Although in vitro assays show sulfurtransferase or phosphatase activity associated with rhodanese or rhodanese-like domains, specific biological roles for most members of this homology superfamily have not been established. RESULTS: Eight ORFs coding for proteins consisting of (or containing) a rhodanese domain bearing the potentially catalytic Cys have been identified in the Escherichia coli K-12 genome. One of these codes for the 12-kDa protein GlpE, a member of the sn-glycerol 3-phosphate (glp) regulon. The crystal structure of GlpE, reported here at 1.06 A resolution, displays alpha/beta topology based on five beta strands and five alpha helices. The GlpE catalytic Cys residue is persulfurated and enclosed in a structurally conserved 5-residue loop in a region of positive electrostatic field. CONCLUSIONS: Relative to the two-domain rhodanese enzymes of known three-dimensional structure, GlpE displays substantial shortening of loops connecting alpha helices and beta sheets, resulting in radical conformational changes surrounding the active site. As a consequence, GlpE is structurally more similar to Cdc25 phosphatases than to bovine or Azotobacter vinelandii rhodaneses. Sequence searches through completed genomes indicate that GlpE can be considered to be the prototype structure for the ubiquitous single-domain rhodanese module. | ||
==About this Structure== | ==About this Structure== | ||
1GN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NA and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1GN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GN0 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Bolognesi, M.]] | [[Category: Bolognesi, M.]] | ||
[[Category: Bordo, D.]] | [[Category: Bordo, D.]] | ||
[[Category: Donahue, J | [[Category: Donahue, J T.]] | ||
[[Category: Larson, T | [[Category: Larson, T J.]] | ||
[[Category: Spallarossa, A.]] | [[Category: Spallarossa, A.]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
| Line 24: | Line 24: | ||
[[Category: sulfurtransferase]] | [[Category: sulfurtransferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:48 2008'' | ||
Revision as of 13:51, 21 February 2008
|
ESCHERICHIA COLI GLPE SULFURTRANSFERASE SOAKED WITH KCN
OverviewOverview
BACKGROUND: Rhodanese domains are structural modules occurring in the three major evolutionary phyla. They are found as single-domain proteins, as tandemly repeated modules in which the C-terminal domain only bears the properly structured active site, or as members of multidomain proteins. Although in vitro assays show sulfurtransferase or phosphatase activity associated with rhodanese or rhodanese-like domains, specific biological roles for most members of this homology superfamily have not been established. RESULTS: Eight ORFs coding for proteins consisting of (or containing) a rhodanese domain bearing the potentially catalytic Cys have been identified in the Escherichia coli K-12 genome. One of these codes for the 12-kDa protein GlpE, a member of the sn-glycerol 3-phosphate (glp) regulon. The crystal structure of GlpE, reported here at 1.06 A resolution, displays alpha/beta topology based on five beta strands and five alpha helices. The GlpE catalytic Cys residue is persulfurated and enclosed in a structurally conserved 5-residue loop in a region of positive electrostatic field. CONCLUSIONS: Relative to the two-domain rhodanese enzymes of known three-dimensional structure, GlpE displays substantial shortening of loops connecting alpha helices and beta sheets, resulting in radical conformational changes surrounding the active site. As a consequence, GlpE is structurally more similar to Cdc25 phosphatases than to bovine or Azotobacter vinelandii rhodaneses. Sequence searches through completed genomes indicate that GlpE can be considered to be the prototype structure for the ubiquitous single-domain rhodanese module.
About this StructureAbout this Structure
1GN0 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily., Spallarossa A, Donahue JL, Larson TJ, Bolognesi M, Bordo D, Structure. 2001 Nov;9(11):1117-25. PMID:11709175
Page seeded by OCA on Thu Feb 21 12:51:48 2008