3t0f: Difference between revisions

Latest revision as of 16:13, 14 March 2024

IspH:HMBPP (substrate) structure of the E126D mutantIspH:HMBPP (substrate) structure of the E126D mutant

Structural highlights

3t0f is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ISPH_ECOLI Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.^[1] ^[2] ^[3]

References

↑ Grawert T, Rohdich F, Span I, Bacher A, Eisenreich W, Eppinger J, Groll M. Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction. Angew Chem Int Ed Engl. 2009;48(31):5756-9. PMID:19569147 doi:10.1002/anie.200900548
↑ Grawert T, Span I, Eisenreich W, Rohdich F, Eppinger J, Bacher A, Groll M. Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1077-81. Epub 2009 Dec 28. PMID:20080550
↑ Span I, Grawert T, Bacher A, Eisenreich W, Groll M. Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis. J Mol Biol. 2011 Nov 23. PMID:22137895 doi:10.1016/j.jmb.2011.11.033

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OCA

[1] Grawert T, Rohdich F, Span I, Bacher A, Eisenreich W, Eppinger J, Groll M. Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction. Angew Chem Int Ed Engl. 2009;48(31):5756-9. PMID:19569147 doi:10.1002/anie.200900548

[2] Grawert T, Span I, Eisenreich W, Rohdich F, Eppinger J, Bacher A, Groll M. Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1077-81. Epub 2009 Dec 28. PMID:20080550

[3] Span I, Grawert T, Bacher A, Eisenreich W, Groll M. Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis. J Mol Biol. 2011 Nov 23. PMID:22137895 doi:10.1016/j.jmb.2011.11.033

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[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3t0f is ON HOLD
+==IspH:HMBPP (substrate) structure of the E126D mutant==
+<StructureSection load='3t0f' size='340' side='right'caption='[[3t0f]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3t0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0F 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</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=3t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0f OCA], [https://pdbe.org/3t0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0f RCSB], [https://www.ebi.ac.uk/pdbsum/3t0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0f ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ISPH_ECOLI ISPH_ECOLI] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.<ref>PMID:19569147</ref> <ref>PMID:20080550</ref> <ref>PMID:22137895</ref>
-Authors: Span, I., Graewert, T., Bacher, A., Eisenreich, W., Groll, M.
+==See Also==
+*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures|4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures]]
-Description: IspH:HMBPP (substrate) structure of the E126D mutant
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Bacher A]]
+[[Category: Eisenreich W]]
+[[Category: Graewert T]]
+[[Category: Groll M]]
+[[Category: Span I]]

3t0f: Difference between revisions

Latest revision as of 16:13, 14 March 2024

IspH:HMBPP (substrate) structure of the E126D mutantIspH:HMBPP (substrate) structure of the E126D mutant

Structural highlights

Function

See Also

References

Contents

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3t0f: Difference between revisions

Latest revision as of 16:13, 14 March 2024

IspH:HMBPP (substrate) structure of the E126D mutantIspH:HMBPP (substrate) structure of the E126D mutant

Structural highlights

Function

See Also

References

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