2g37
From Proteopedia
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|PDB= 2g37 |SIZE=350|CAPTION= <scene name='initialview01'>2g37</scene>, resolution 2.000Å | |PDB= 2g37 |SIZE=350|CAPTION= <scene name='initialview01'>2g37</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | |GENE= proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g37 OCA], [http://www.ebi.ac.uk/pdbsum/2g37 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g37 RCSB]</span> | ||
}} | }} | ||
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[[Category: Tanner, J J.]] | [[Category: Tanner, J J.]] | ||
[[Category: White, T A.]] | [[Category: White, T A.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: MPD]] | ||
[[Category: beta8-alpha8-barrel]] | [[Category: beta8-alpha8-barrel]] | ||
[[Category: flavoenzyme]] | [[Category: flavoenzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:11:12 2008'' |
Revision as of 00:11, 31 March 2008
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| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase (Thermus thermophilus) | ||||||
| Activity: | Proline dehydrogenase, with EC number 1.5.99.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Thermus thermophilus L-proline dehydrogenase
Overview
Proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the two-step oxidation of proline to glutamate. They are distinct monofunctional enzymes in all eukaryotes and some bacteria but are fused into bifunctional enzymes known as proline utilization A (PutA) in other bacteria. Here we report the first structure and biochemical data for a monofunctional PRODH. The 2.0-A resolution structure of Thermus thermophilus PRODH reveals a distorted (betaalpha)(8) barrel catalytic core domain and a hydrophobic alpha-helical domain located above the carboxyl-terminal ends of the strands of the barrel. Although the catalytic core is similar to that of the PutA PRODH domain, the FAD conformation of T. thermophilus PRODH is remarkably different and likely reflects unique requirements for membrane association and communication with P5CDH. Also, the FAD of T. thermophilus PRODH is highly solvent-exposed compared with PutA due to a 4-A shift of helix 8. Structure-based sequence analysis of the PutA/PRODH family led us to identify nine conserved motifs involved in cofactor and substrate recognition. Biochemical studies show that the midpoint potential of the FAD is -75 mV and the kinetic parameters for proline are K(m) = 27 mm and k(cat) = 13 s(-1). 3,4-Dehydro-l-proline was found to be an efficient substrate, and l-tetrahydro-2-furoic acid is a competitive inhibitor (K(I) = 1.0 mm). Finally, we demonstrate that T. thermophilus PRODH reacts with O(2) producing superoxide. This is significant because superoxide production underlies the role of human PRODH in p53-mediated apoptosis, implying commonalities between eukaryotic and bacterial monofunctional PRODHs.
About this Structure
2G37 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structure and kinetics of monofunctional proline dehydrogenase from Thermus thermophilus., White TA, Krishnan N, Becker DF, Tanner JJ, J Biol Chem. 2007 May 11;282(19):14316-27. Epub 2007 Mar 7. PMID:17344208
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