2pi8: Difference between revisions
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|PDB= 2pi8 |SIZE=350|CAPTION= <scene name='initialview01'>2pi8</scene>, resolution 2.250Å | |PDB= 2pi8 |SIZE=350|CAPTION= <scene name='initialview01'>2pi8</scene>, resolution 2.250Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mltA, mlt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= mltA, mlt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK11162 mltA], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam03562 MltA], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam06725 3D]</span> | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pi8 OCA], [http://www.ebi.ac.uk/pdbsum/2pi8 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2pi8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Straaten, K E.van.]] | [[Category: Straaten, K E.van.]] | ||
[[Category: Thunnissen, A M.W H.]] | [[Category: Thunnissen, A M.W H.]] | ||
[[Category: double-psi beta-barrel]] | |||
[[Category: double-psi beta-barrel | |||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: lytic transglycosylase]] | |||
[[Category: protein-sugar complex]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:39:46 2008'' | ||
Revision as of 07:39, 26 March 2008
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| , resolution 2.250Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | mltA, mlt (Escherichia coli) | ||||||
| Domains: | mltA, MltA, 3D | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of E. coli MltA with bound chitohexaose
OverviewOverview
Crystal structures of an inactive mutant (D308A) of the lytic transglycosylase MltA from Escherichia coli have been determined in two different apo-forms, as well as in complex with the substrate analogue chitohexaose. The chitohexaose binds with all six saccharide residues in the active site groove, with an intact glycosidic bond at the bond cleavage center. Its binding induces a large reorientation of the two structural domains in MltA, narrowing the active site groove and allowing tight interactions of the oligosaccharide with residues from both domains. The structures identify residues in MltA with key roles in the binding and recognition of peptidoglycan and confirm that Asp-308 is the single catalytic residue, acting as a general acid/base. Moreover, the structures suggest that catalysis involves a high energy conformation of the scissile glycosidic linkage and that the putative oxocarbenium ion intermediate is stabilized by the dipole moment of a nearby alpha-helix.
About this StructureAbout this Structure
2PI8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure of Escherichia coli Lytic transglycosylase MltA with bound chitohexaose: implications for peptidoglycan binding and cleavage., van Straaten KE, Barends TR, Dijkstra BW, Thunnissen AM, J Biol Chem. 2007 Jul 20;282(29):21197-205. Epub 2007 May 14. PMID:17502382
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