2fa1
From Proteopedia
(New page: 200px<br /><applet load="2fa1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fa1, resolution 1.70Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2fa1.gif|left|200px]]<br /><applet load="2fa1" size=" | + | [[Image:2fa1.gif|left|200px]]<br /><applet load="2fa1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fa1, resolution 1.70Å" /> | caption="2fa1, resolution 1.70Å" /> | ||
'''Crystal structure of PhnF C-terminal domain'''<br /> | '''Crystal structure of PhnF C-terminal domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) | + | The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 A resolution by the single wavelength anomalous dispersion (SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N-terminal DNA-binding domains, but are divided into four subfamilies according to their heterogenic C-terminal domains, which are involved in effector binding and oligomerization. The C-PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR-like regulators. The structure represents a mixture of alpha-helices and beta-strands, with a six-stranded antiparallel beta-sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand beta-sheets that include core antiparallel and N-terminal two-strand parallel beta-sheets from each monomer. C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops. The structural comparison of the C-PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding. |
==About this Structure== | ==About this Structure== | ||
| - | 2FA1 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 BDF as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FA1 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=BDF:'>BDF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FA1 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Edwards, A | + | [[Category: Edwards, A M.]] |
[[Category: Gorelik, M.]] | [[Category: Gorelik, M.]] | ||
| - | [[Category: Lunin, V | + | [[Category: Lunin, V V.]] |
| - | [[Category: MCSG, Midwest | + | [[Category: MCSG, Midwest Center for Structural Genomics.]] |
| - | [[Category: Nocek, B | + | [[Category: Nocek, B P.]] |
[[Category: Savchenko, A.]] | [[Category: Savchenko, A.]] | ||
[[Category: Skarina, T.]] | [[Category: Skarina, T.]] | ||
| Line 31: | Line 31: | ||
[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:16 2008'' |
Revision as of 15:19, 21 February 2008
|
Crystal structure of PhnF C-terminal domain
Overview
The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 A resolution by the single wavelength anomalous dispersion (SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N-terminal DNA-binding domains, but are divided into four subfamilies according to their heterogenic C-terminal domains, which are involved in effector binding and oligomerization. The C-PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR-like regulators. The structure represents a mixture of alpha-helices and beta-strands, with a six-stranded antiparallel beta-sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand beta-sheets that include core antiparallel and N-terminal two-strand parallel beta-sheets from each monomer. C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops. The structural comparison of the C-PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding.
About this Structure
2FA1 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Structural characterization of GntR/HutC family signaling domain., Gorelik M, Lunin VV, Skarina T, Savchenko A, Protein Sci. 2006 Jun;15(6):1506-11. Epub 2006 May 2. PMID:16672238
Page seeded by OCA on Thu Feb 21 17:19:16 2008
Categories: Escherichia coli | Single protein | Edwards, A M. | Gorelik, M. | Lunin, V V. | MCSG, Midwest Center for Structural Genomics. | Nocek, B P. | Savchenko, A. | Skarina, T. | BDF | Apc5558 | Effector binding domain | Mcsg | Midwest center for structural genomics | Pnhf | Protein structure initiative | Psi | Regulator | Transcription
