3du0
From Proteopedia
(Difference between revisions)
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==E. coli dihydrodipicolinate synthase with first substrate, pyruvate, bound in active site== | ==E. coli dihydrodipicolinate synthase with first substrate, pyruvate, bound in active site== | ||
| - | <StructureSection load='3du0' size='340' side='right' caption='[[3du0]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3du0' size='340' side='right'caption='[[3du0]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3du0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DU0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DU0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3du0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DU0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DU0 FirstGlance]. <br> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3du0 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3du0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)-lysine and meso-diaminopimelate, molecules which play a crucial cross-linking role in bacterial cell walls. An effective inhibitor of DHDPS would represent a useful antibacterial agent; despite extensive effort, a suitable inhibitor has yet to be found. In an attempt to examine the specificity of the active site of DHDPS, the enzyme was cocrystallized with the substrate analogue oxaloacetate. The resulting crystals diffracted to 2.0 A resolution, but solution of the protein structure revealed that pyruvate was bound in the active site rather than oxaloacetic acid. Kinetic analysis confirmed that the decarboxylation of oxaloacetate was not catalysed by DHDPS and was instead a slow spontaneous chemical process. | ||
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| + | The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate.,Devenish SR, Gerrard JA, Jameson GB, Dobson RC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 1;64(Pt 12):1092-5., doi: 10.1107/S1744309108033654. Epub 2008 Nov 28. PMID:19052357<ref>PMID:19052357</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3du0" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | [[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Devenish, S R.A]] | [[Category: Devenish, S R.A]] | ||
[[Category: Dobson, R C.J]] | [[Category: Dobson, R C.J]] | ||
Revision as of 08:08, 18 December 2019
E. coli dihydrodipicolinate synthase with first substrate, pyruvate, bound in active site
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