000 01638 a2200457 4500
005 20250514215915.0
264 0 _c20050712
008 200507s 0 0 eng d
022 _a0021-9258
024 7 _a10.1074/jbc.M413799200
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aMathieu, Magali
245 0 0 _aEscherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cMay 2005
300 _a18916-22 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAdenosine Triphosphate
_xchemistry
650 0 4 _aAnti-Infective Agents
_xpharmacology
650 0 4 _aBinding Sites
650 0 4 _aCatalysis
650 0 4 _aCatalytic Domain
650 0 4 _aCrystallography, X-Ray
650 0 4 _aEscherichia coli
_xenzymology
650 0 4 _aEscherichia coli Proteins
650 0 4 _aLactobacillus
_xenzymology
650 0 4 _aModels, Chemical
650 0 4 _aModels, Molecular
650 0 4 _aMultienzyme Complexes
_xchemistry
650 0 4 _aPeptide Synthases
_xchemistry
650 0 4 _aProtein Binding
650 0 4 _aProtein Conformation
650 0 4 _aProtein Structure, Secondary
650 0 4 _aPterins
_xchemistry
700 1 _aDebousker, Guy
700 1 _aVincent, Sophie
700 1 _aViviani, Fabrice
700 1 _aBamas-Jacques, Nathalie
700 1 _aMikol, Vincent
773 0 _tThe Journal of biological chemistry
_gvol. 280
_gno. 19
_gp. 18916-22
856 4 0 _uhttps://doi.org/10.1074/jbc.M413799200
_zAvailable from publisher's website
999 _c15381774
_d15381774