4a52
From Proteopedia
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| - | [[Image:4a52.png|left|200px]] | ||
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{{STRUCTURE_4a52| PDB=4a52 | SCENE= }} | {{STRUCTURE_4a52| PDB=4a52 | SCENE= }} | ||
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===NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis=== | ===NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis=== | ||
| + | {{ABSTRACT_PUBMED_22579252}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/YKUD_BACSU YKUD_BACSU]] Probable enzyme that may play an important role in cell wall biology.<ref>PMID:16287140</ref> | ||
==About this Structure== | ==About this Structure== | ||
| - | [[4a52]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4a52]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A52 OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:022579252</ref><references group="xtra"/> | + | <ref group="xtra">PMID:022579252</ref><references group="xtra"/><references/> |
| - | [[Category: | + | [[Category: Bacsu]] |
[[Category: Arthur, M.]] | [[Category: Arthur, M.]] | ||
[[Category: Bougault, C.]] | [[Category: Bougault, C.]] | ||
Revision as of 07:05, 15 January 2014
Contents |
NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis
Template:ABSTRACT PUBMED 22579252
Function
[YKUD_BACSU] Probable enzyme that may play an important role in cell wall biology.[1]
About this Structure
4a52 is a 1 chain structure with sequence from Bacsu. Full experimental information is available from OCA.
Reference
- Lecoq L, Bougault C, Hugonnet JE, Veckerle C, Pessey O, Arthur M, Simorre JP. Dynamics Induced by beta-Lactam Antibiotics in the Active Site of Bacillus subtilisl,d-Transpeptidase. Structure. 2012 May 9;20(5):850-61. PMID:22579252 doi:10.1016/j.str.2012.03.015
- ↑ Bielnicki J, Devedjiev Y, Derewenda U, Dauter Z, Joachimiak A, Derewenda ZS. B. subtilis ykuD protein at 2.0 A resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes. Proteins. 2006 Jan 1;62(1):144-51. PMID:16287140 doi:10.1002/prot.20702
