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{{STRUCTURE_4jh9|  PDB=4jh9  |  SCENE=  }}
===Crystal Structure of FosB from Bacillus cereus with Maganese and Potential BSH-Fosfomycin Product===
{{ABSTRACT_PUBMED_24004181}}


==Function==
==Crystal Structure of FosB from Bacillus cereus with Maganese and Potential BSH-Fosfomycin Product==
[[http://www.uniprot.org/uniprot/FOSB_BACC1 FOSB_BACC1]] Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor (By similarity).  
<StructureSection load='4jh9' size='340' side='right'caption='[[4jh9]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jh9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_10987 Bacillus cereus ATCC 10987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JH9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1KM:(2R)-2-AZANYL-3-[(1R,2S)-2-OXIDANYL-1-PHOSPHONO-PROPYL]SULFANYL-PROPANOIC+ACID'>1KM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jh9 OCA], [https://pdbe.org/4jh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jh9 RCSB], [https://www.ebi.ac.uk/pdbsum/4jh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jh9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FOSB_BACC1 FOSB_BACC1] Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor (By similarity).


==About this Structure==
==See Also==
[[4jh9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_atcc_10987 Bacillus cereus atcc 10987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JH9 OCA].
*[[Metallothiol transferase FosB|Metallothiol transferase FosB]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:024004181</ref><references group="xtra"/><references/>
[[Category: Bacillus cereus ATCC 10987]]
[[Category: Bacillus cereus atcc 10987]]
[[Category: Large Structures]]
[[Category: Armstrong, R N.]]
[[Category: Armstrong RN]]
[[Category: Cook, P D.]]
[[Category: Cook PD]]
[[Category: Harp, J.]]
[[Category: Harp J]]
[[Category: Jagessar, K.]]
[[Category: Jagessar K]]
[[Category: Keithly, M E.]]
[[Category: Keithly ME]]
[[Category: Thompson, M K.]]
[[Category: Thompson MK]]
[[Category: Bacillithiol-s-transferase]]
[[Category: Transferase-transferase inhibitor complex]]

Latest revision as of 15:03, 1 March 2024

Crystal Structure of FosB from Bacillus cereus with Maganese and Potential BSH-Fosfomycin ProductCrystal Structure of FosB from Bacillus cereus with Maganese and Potential BSH-Fosfomycin Product

Structural highlights

4jh9 is a 2 chain structure with sequence from Bacillus cereus ATCC 10987. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.77Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FOSB_BACC1 Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor (By similarity).

See Also

4jh9, resolution 1.77Å

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