1b93: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1b93.gif|left|200px]] | [[Image:1b93.gif|left|200px]] | ||
'''METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI''' | {{Structure | ||
|PDB= 1b93 |SIZE=350|CAPTION= <scene name='initialview01'>1b93</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Methylglyoxal_synthase Methylglyoxal synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.3 4.2.3.3] | |||
|GENE= MGSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI''' | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1B93 is a [ | 1B93 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=1B93 OCA]. | ||
==Reference== | ==Reference== | ||
The crystal structure of methylglyoxal synthase from Escherichia coli., Saadat D, Harrison DH, Structure. 1999 Mar 15;7(3):309-17. PMID:[http:// | The crystal structure of methylglyoxal synthase from Escherichia coli., Saadat D, Harrison DH, Structure. 1999 Mar 15;7(3):309-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10368300 10368300] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Methylglyoxal synthase]] | [[Category: Methylglyoxal synthase]] | ||
Line 22: | Line 31: | ||
[[Category: methylglyoxal]] | [[Category: methylglyoxal]] | ||
''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 10:07:52 2008'' |
Revision as of 11:07, 20 March 2008
| |||||||
, resolution 1.90Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | and | ||||||
Gene: | MGSA (Escherichia coli) | ||||||
Activity: | Methylglyoxal synthase, with EC number 4.2.3.3 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI
OverviewOverview
BACKGROUND: The reaction mechanism of methylglyoxal synthase (MGS) is believed to be similar to that of triosephosphate isomerase (TIM). Both enzymes utilise dihydroxyacetone phosphate (DHAP) to form an enediol(ate) phosphate intermediate as the first step of their reaction pathways. However, the second catalytic step in the MGS reaction pathway is characterized by the elimination of phosphate and collapse of the enediol(ate) to form methylglyoxal instead of reprotonation to form the isomer glyceraldehyde 3-phosphate. RESULTS: The crystal structure of MGS bound to formate and substoichiometric amounts of phosphate in the space group P6522 has been determined at 1.9 A resolution. This structure shows that the enzyme is a homohexamer composed of interacting five-stranded beta/alpha proteins, rather than the hallmark alpha/beta barrel structure of TIM. The conserved residues His19, Asp71, and His98 in each of the three monomers in the asymmetric unit bind to a formate ion that is present in the crystallization conditions. Differences in the three monomers in the asymmetric unit are localized at the mouth of the active site and can be ascribed to the presence or absence of a bound phosphate ion. CONCLUSIONS: In agreement with site-directed mutagenesis and mechanistic enzymology, the structure suggests that Asp71 acts as the catalytic base. Further, Asp20 and Asp101 are involved in intersubunit salt bridges. These salt bridges may provide a pathway for transmitting allosteric information.
About this StructureAbout this Structure
1B93 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of methylglyoxal synthase from Escherichia coli., Saadat D, Harrison DH, Structure. 1999 Mar 15;7(3):309-17. PMID:10368300
Page seeded by OCA on Thu Mar 20 10:07:52 2008