1d0l

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|PDB= 1d0l |SIZE=350|CAPTION= <scene name='initialview01'>1d0l</scene>, resolution 1.97&Aring;
|PDB= 1d0l |SIZE=350|CAPTION= <scene name='initialview01'>1d0l</scene>, resolution 1.97&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=BLG:4-O-(4-O-SULFONYL-N-ACETYLGLUCOSAMININYL)-5-METHYLHYDROXY-L-PROLINE-TAURINE'>BLG</scene>
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|LIGAND= <scene name='pdbligand=BLG:4-O-(4-O-SULFONYL-N-ACETYLGLUCOSAMININYL)-5-METHYLHYDROXY-L-PROLINE-TAURINE'>BLG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1qus|1QUS]], [[1qut|1QUT]], [[1qdr|1QDR]], [[1qdt|1QDT]], [[1d0k|1D0K]], [[1d0l|1D0L]], [[1d0m|1D0M]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0l OCA], [http://www.ebi.ac.uk/pdbsum/1d0l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d0l RCSB]</span>
}}
}}
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[[Category: Dijkstra, B W.]]
[[Category: Dijkstra, B W.]]
[[Category: Kalk, K H.]]
[[Category: Kalk, K H.]]
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[[Category: BLG]]
 
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[[Category: CA]]
 
[[Category: alpha-helical protein with a five stranded anti-parallel beta-sheet]]
[[Category: alpha-helical protein with a five stranded anti-parallel beta-sheet]]
[[Category: ef-hand]]
[[Category: ef-hand]]
[[Category: glycosyl transferase]]
[[Category: glycosyl transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:31:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:32:08 2008''

Revision as of 16:32, 30 March 2008


PDB ID 1d0l

Drag the structure with the mouse to rotate
, resolution 1.97Å
Ligands: ,
Related: 1QUS, 1QUT, 1QDR, 1QDT, 1D0K, 1D0L, 1D0M


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A


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.

About this Structure

1D0L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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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