1ylh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ylh.gif|left|200px]] | [[Image:1ylh.gif|left|200px]] | ||
'''Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate''' | {{Structure | ||
|PDB= 1ylh |SIZE=350|CAPTION= <scene name='initialview01'>1ylh</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=DT3:(2S,3S)-2,3-DIHYDROXY-4-SULFANYLBUTANE-1-SULFONATE'>DT3</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(ATP) Phosphoenolpyruvate carboxykinase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.49 4.1.1.49] | |||
|GENE= PCKA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67854 Actinobacillus succinogenes]) | |||
}} | |||
'''Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1YLH is a [ | 1YLH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Actinobacillus_succinogenes Actinobacillus succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YLH OCA]. | ||
==Reference== | ==Reference== | ||
Structure of PEP carboxykinase from the succinate-producing Actinobacillus succinogenes: a new conserved active-site motif., Leduc YA, Prasad L, Laivenieks M, Zeikus JG, Delbaere LT, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):903-12. Epub 2005, Jun 24. PMID:[http:// | Structure of PEP carboxykinase from the succinate-producing Actinobacillus succinogenes: a new conserved active-site motif., Leduc YA, Prasad L, Laivenieks M, Zeikus JG, Delbaere LT, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):903-12. Epub 2005, Jun 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15983413 15983413] | ||
[[Category: Actinobacillus succinogenes]] | [[Category: Actinobacillus succinogenes]] | ||
[[Category: Phosphoenolpyruvate carboxykinase (ATP)]] | [[Category: Phosphoenolpyruvate carboxykinase (ATP)]] | ||
| Line 29: | Line 38: | ||
[[Category: phosphoenolpyruvate carboxykinase]] | [[Category: phosphoenolpyruvate carboxykinase]] | ||
''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 15:24:24 2008'' | ||
Revision as of 16:24, 20 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , and | ||||||
| Gene: | PCKA (Actinobacillus succinogenes) | ||||||
| Activity: | Phosphoenolpyruvate carboxykinase (ATP), with EC number 4.1.1.49 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Phosphoenolpyruvate Carboxykinase from Actinobaccilus succinogenes in Complex with Manganese and Pyruvate
OverviewOverview
Actinobacillus succinogenes can produce, via fermentation, high concentrations of succinate, an important industrial commodity. A key enzyme in this pathway is phosphoenolpyruvate carboxykinase (PCK), which catalyzes the production of oxaloacetate from phosphoenolpyruvate and carbon dioxide, with the concomitant conversion of adenosine 5'-diphosphate to adenosine 5'-triphosphate. 1.85 and 1.70 A resolution structures of the native and a pyruvate/Mn(2+)/phosphate complex have been solved, respectively. The structure of the complex contains sulfhydryl reducing agents covalently bound to three cysteine residues via disulfide bonds. One of these cysteine residues (Cys285) is located in the active-site cleft and may be analogous to the putative reactive cysteine of PCK from Trypanosoma cruzi. Cys285 is also part of a previously unreported conserved motif comprising residues 280-287 and containing the pattern NXEXGXY(/F)A(/G); this new motif appears to have a structural role in stabilizing and positioning side chains that bind substrates and metal ions. The first few residues of this motif connect the two domains of the enzyme and a fulcrum point appears to be located near Asn280. In addition, an active-site Asp residue forms two coordinate bonds with the Mn(2+) ion present in the structure of the complex in a symmetrical bidentate manner, unlike in other PCK structures that contain a manganese ion.
About this StructureAbout this Structure
1YLH is a Single protein structure of sequence from Actinobacillus succinogenes. Full crystallographic information is available from OCA.
ReferenceReference
Structure of PEP carboxykinase from the succinate-producing Actinobacillus succinogenes: a new conserved active-site motif., Leduc YA, Prasad L, Laivenieks M, Zeikus JG, Delbaere LT, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):903-12. Epub 2005, Jun 24. PMID:15983413
Page seeded by OCA on Thu Mar 20 15:24:24 2008