4knl

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m (Protected "4knl" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4knl| PDB=4knl | SCENE= }}
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===Crystal structure of Staphylococcus aureus hydrolase AmiA in complex with its ligand===
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The entry 4knl is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/ATL_STAA8 ATL_STAA8]] Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity).
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Authors: Buettner, F.M., Stehle, T.
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==About this Structure==
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[[4knl]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KNL OCA].
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Description:
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[[Category: Buettner, F M.]]
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[[Category: Stehle, T.]]
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[[Category: Amidase]]
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[[Category: Autolysin]]
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[[Category: Hydrolase-substrate complex]]
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[[Category: Ligand complex]]
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[[Category: N-acetylmuramoyl-l-alanine amidase]]
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[[Category: Peptidoglycan]]

Revision as of 13:58, 12 March 2014

Template:STRUCTURE 4knl

Crystal structure of Staphylococcus aureus hydrolase AmiA in complex with its ligand

Function

[ATL_STAA8] Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity).

About this Structure

4knl is a 6 chain structure. Full crystallographic information is available from OCA.

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OCA

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