2fzm
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2fzm.jpg|left|200px]] | + | [[Image:2fzm.jpg|left|200px]] |
| - | + | ||
| - | '''Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and complexed with SO2''' | + | {{Structure |
| + | |PDB= 2fzm |SIZE=350|CAPTION= <scene name='initialview01'>2fzm</scene>, resolution 2.300Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=SO2:SULFUR DIOXIDE'>SO2</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Proline_dehydrogenase Proline dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.8 1.5.99.8] | ||
| + | |GENE= putA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and complexed with SO2''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2FZM is a [ | + | 2FZM 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=2FZM OCA]. |
==Reference== | ==Reference== | ||
| - | Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA--membrane binding., Zhang W, Zhang M, Zhu W, Zhou Y, Wanduragala S, Rewinkel D, Tanner JJ, Becker DF, Biochemistry. 2007 Jan 16;46(2):483-91. PMID:[http:// | + | Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA--membrane binding., Zhang W, Zhang M, Zhu W, Zhou Y, Wanduragala S, Rewinkel D, Tanner JJ, Becker DF, Biochemistry. 2007 Jan 16;46(2):483-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17209558 17209558] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Proline dehydrogenase]] | [[Category: Proline dehydrogenase]] | ||
| Line 21: | Line 30: | ||
[[Category: proline catabolism]] | [[Category: proline catabolism]] | ||
[[Category: proline dehydrogenase]] | [[Category: proline dehydrogenase]] | ||
| - | [[Category: proline utilization | + | [[Category: proline utilization some]] |
[[Category: puta]] | [[Category: puta]] | ||
| - | ''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 16:58:42 2008'' |
Revision as of 14:58, 20 March 2008
| |||||||
| , resolution 2.300Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | putA (Escherichia coli) | ||||||
| Activity: | Proline dehydrogenase, with EC number 1.5.99.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and complexed with SO2
Overview
PutA is a novel flavoprotein in Escherichia coli that switches from a transcriptional repressor to a membrane-bound proline catabolic enzyme. Previous crystallographic studies of the PutA proline dehydrogenase (PRODH) domain under oxidizing conditions revealed that FAD N(5) and the ribityl 2'-OH group form hydrogen bonds with Arg431 and Arg556, respectively. Here we identify molecular interactions in the PutA PRODH active site that underlie redox-dependent functional switching of PutA. We report that reduction of the PRODH domain induces major structural changes in the FAD cofactor, including a 22 degrees bend of the isoalloxazine ring along the N(5)-N(10) axis, crankshaft rotation of the upper part of the ribityl chain, and formation of a new hydrogen bond network involving the ribityl 2'-OH group, FAD N(1), and Gly435. The roles of the FAD 2'-OH group and the FAD N(5)-Arg431 hydrogen bond pair in regulating redox-dependent PutA-membrane associations were tested using FAD analogues and site-directed mutagenesis. Kinetic membrane binding measurements and cell-based reporter gene assays of modified PutA proteins show that disrupting the FAD N(5)-Arg431 interaction impairs the reductive activation of PutA-membrane binding. We also show that the FAD 2'-OH group acts as a redox-sensitive toggle switch that controls PutA-membrane binding. These results illustrate a new versatility of the ribityl chain in flavoprotein mechanisms.
About this Structure
2FZM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA--membrane binding., Zhang W, Zhang M, Zhu W, Zhou Y, Wanduragala S, Rewinkel D, Tanner JJ, Becker DF, Biochemistry. 2007 Jan 16;46(2):483-91. PMID:17209558
Page seeded by OCA on Thu Mar 20 16:58:42 2008
