2hna
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2hna.gif|left|200px]] | + | [[Image:2hna.gif|left|200px]] |
| - | + | ||
| - | '''Solution Structure of a bacterial apo-flavodoxin''' | + | {{Structure |
| + | |PDB= 2hna |SIZE=350|CAPTION= <scene name='initialview01'>2hna</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution Structure of a bacterial apo-flavodoxin''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2HNA is a [ | + | 2HNA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNA OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both Apo- and Holo-forms: implications for cofactor binding and electron transfer., Hu Y, Li Y, Zhang X, Guo X, Xia B, Jin C, J Biol Chem. 2006 Nov 17;281(46):35454-66. Epub 2006 Sep 8. PMID:[http:// | + | Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both Apo- and Holo-forms: implications for cofactor binding and electron transfer., Hu Y, Li Y, Zhang X, Guo X, Xia B, Jin C, J Biol Chem. 2006 Nov 17;281(46):35454-66. Epub 2006 Sep 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16963438 16963438] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 18: | Line 27: | ||
[[Category: flavodoxin fold]] | [[Category: flavodoxin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:08 2008'' |
Revision as of 15:19, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure of a bacterial apo-flavodoxin
Overview
Flavodoxins play central roles in the electron transfer involving various biological processes in microorganisms. The mioC gene of Escherichia coli encodes a 16-kDa flavodoxin and locates next to the chromosomal replication initiation origin (oriC). Extensive researches have been carried out to investigate the relationship between mioC transcription and replication initiation. Recently, the MioC protein was proposed to be essential for the biotin synthase activity in vitro. Nevertheless, the exact role of MioC in biotin synthesis and its physiological function in vivo remain elusive. In order to understand the molecular basis of the biological functions of MioC and the cofactor-binding mechanisms of flavodoxins, we have determined the solution structures of both the apo- and holo-forms of E. coli MioC protein at high resolution by nuclear magnetic resonance spectroscopy. The overall structures of both forms consist of an alpha/beta sandwich, which highly resembles the classical flavodoxin fold. However, significant diversities are observed between the two forms, especially the stabilization of the FMN-binding loops and the notable extension of secondary structures upon FMN binding. Structural comparison reveals fewer negative charged and aromatic residues near the FMN-binding site of MioC, as compared with that of flavodoxin 1 from E. coli, which may affect both the redox potentials and the redox partner interactions. Furthermore, the backbone dynamics studies reveal the conformational flexibility at different time scales for both apo- and holo-forms of MioC, which may play important roles for cofactor binding and electron transfer.
About this Structure
2HNA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both Apo- and Holo-forms: implications for cofactor binding and electron transfer., Hu Y, Li Y, Zhang X, Guo X, Xia B, Jin C, J Biol Chem. 2006 Nov 17;281(46):35454-66. Epub 2006 Sep 8. PMID:16963438
Page seeded by OCA on Thu Mar 20 17:19:08 2008
