1b93: Difference between revisions

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[[Image:1b93.gif|left|200px]]<br /><applet load="1b93" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1b93.gif|left|200px]]
caption="1b93, resolution 1.90&Aring;" />
 
'''METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI'''<br />
{{Structure
|PDB= 1b93 |SIZE=350|CAPTION= <scene name='initialview01'>1b93</scene>, resolution 1.90&Aring;
|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==
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==About this Structure==
==About this Structure==
1B93 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B93 OCA].  
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368300 10368300]
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]]
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[[Category: methylglyoxal]]
[[Category: methylglyoxal]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:49 2008''
''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

File:1b93.gif


PDB ID 1b93

Drag the structure with the mouse to rotate
, 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

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