1d0m: Difference between revisions

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New page: left|200px<br /><applet load="1d0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0m, resolution 2.47Å" /> '''THE ESCHERICHIA COLI...
 
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[[Image:1d0m.jpg|left|200px]]<br /><applet load="1d0m" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1d0m.jpg|left|200px]]<br /><applet load="1d0m" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1d0m, resolution 2.47&Aring;" />
caption="1d0m, resolution 2.47&Aring;" />
'''THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A AND (GLCNAC)2'''<br />
'''THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A AND (GLCNAC)2'''<br />


==Overview==
==Overview==
Lytic transglycosylases catalyze the cleavage of the beta-1, 4-glycosidic, bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine, (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydro bond, in the MurNAc residue. To understand the reaction mechanism of Escherichia, coli lytic transglycosylase Slt35, three crystal structures have been, determined of Slt35 in complex with two different peptidoglycan fragments, and with the lytic transglycosylase inhibitor bulgecin A. The complexes, define four sugar-binding subsites (-2, -1, +1, and +2) and two, peptide-binding sites in a large cleft close to Glu162. The Glu162 side, chain is between the -1 and +1 sugar-binding sites, in agreement with a, function as catalytic acid/base. The complexes suggest additional, contributions to catalysis from Ser216 and Asn339, residues which are, conserved among the MltB/Slt35 lytic transglycosylases.
Lytic transglycosylases catalyze the cleavage of the beta-1, 4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydro bond in the MurNAc residue. To understand the reaction mechanism of Escherichia coli lytic transglycosylase Slt35, three crystal structures have been determined of Slt35 in complex with two different peptidoglycan fragments and with the lytic transglycosylase inhibitor bulgecin A. The complexes define four sugar-binding subsites (-2, -1, +1, and +2) and two peptide-binding sites in a large cleft close to Glu162. The Glu162 side chain is between the -1 and +1 sugar-binding sites, in agreement with a function as catalytic acid/base. The complexes suggest additional contributions to catalysis from Ser216 and Asn339, residues which are conserved among the MltB/Slt35 lytic transglycosylases.


==About this Structure==
==About this Structure==
1D0M 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 CA and BLG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D0M OCA].  
1D0M 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=CA:'>CA</scene> and <scene name='pdbligand=BLG:'>BLG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D0M OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Asselt, E.J.van.]]
[[Category: Asselt, E J.van.]]
[[Category: Dijkstra, B.W.]]
[[Category: Dijkstra, B W.]]
[[Category: Kalk, K.H.]]
[[Category: Kalk, K H.]]
[[Category: BLG]]
[[Category: BLG]]
[[Category: CA]]
[[Category: CA]]
Line 22: Line 22:
[[Category: glycosyl transferase]]
[[Category: glycosyl transferase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:54:48 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:45 2008''

Revision as of 13:11, 21 February 2008

File:1d0m.jpg


1d0m, resolution 2.47Å

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THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A AND (GLCNAC)2

OverviewOverview

Lytic transglycosylases catalyze the cleavage of the beta-1, 4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydro bond in the MurNAc residue. To understand the reaction mechanism of Escherichia coli lytic transglycosylase Slt35, three crystal structures have been determined of Slt35 in complex with two different peptidoglycan fragments and with the lytic transglycosylase inhibitor bulgecin A. The complexes define four sugar-binding subsites (-2, -1, +1, and +2) and two peptide-binding sites in a large cleft close to Glu162. The Glu162 side chain is between the -1 and +1 sugar-binding sites, in agreement with a function as catalytic acid/base. The complexes suggest additional contributions to catalysis from Ser216 and Asn339, residues which are conserved among the MltB/Slt35 lytic transglycosylases.

About this StructureAbout this Structure

1D0M is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan., van Asselt EJ, Kalk KH, Dijkstra BW, Biochemistry. 2000 Feb 29;39(8):1924-34. PMID:10684641

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