3sfm: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Novel crystallization conditions for tandem variant R67 DHFR yields wild-type crystal structure==
==Novel crystallization conditions for tandem variant R67 DHFR yields wild-type crystal structure==
<StructureSection load='3sfm' size='340' side='right' caption='[[3sfm]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='3sfm' size='340' side='right'caption='[[3sfm]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3sfm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SFM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SFM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3sfm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SFM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dfrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></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=3sfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sfm OCA], [https://pdbe.org/3sfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sfm RCSB], [https://www.ebi.ac.uk/pdbsum/3sfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sfm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sfm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sfm RCSB], [http://www.ebi.ac.uk/pdbsum/3sfm PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/DYR21_ECOLX DYR21_ECOLX] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
Trimethoprim is an antibiotic that targets bacterial dihydrofolate reductase (DHFR). A plasmid-encoded DHFR known as R67 DHFR provides resistance to trimethoprim in bacteria. To better understand the mechanism of this homotetrameric enzyme, a tandem dimer construct was created that linked two monomeric R67 DHFR subunits together and mutated the sequence of residues 66-69 of the first subunit from VQIY to INSF. Using a modified crystallization protocol for this enzyme that included in situ proteolysis using chymotrypsin, the tandem dimer was crystallized and the structure was solved at 1.4 A resolution. Surprisingly, only wild-type protomers were incorporated into the crystal. Further experiments demonstrated that the variant protomer was selectively degraded by chymotrypsin, although no canonical chymotrypsin cleavage site had been introduced by these mutations.
 
Novel crystallization conditions for tandem variant R67 DHFR yield a wild-type crystal structure.,Yachnin BJ, Colin DY, Volpato JP, Ebert M, Pelletier JN, Berghuis AM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt, 11):1316-22. Epub 2011 Oct 25. PMID:22102224<ref>PMID:22102224</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Dihydrofolate reductase|Dihydrofolate reductase]]
*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dihydrofolate reductase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Berghuis, A M]]
[[Category: Large Structures]]
[[Category: Yachnin, B J]]
[[Category: Berghuis AM]]
[[Category: Antibiotic resistance]]
[[Category: Yachnin BJ]]
[[Category: Dhf and nadph-binding]]
[[Category: In situ proteolysis]]
[[Category: Oxidoreductase]]
[[Category: Reductase]]
[[Category: Sh3]]
[[Category: Type ii dhfr]]

Latest revision as of 15:55, 14 March 2024

Novel crystallization conditions for tandem variant R67 DHFR yields wild-type crystal structureNovel crystallization conditions for tandem variant R67 DHFR yields wild-type crystal structure

Structural highlights

3sfm is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DYR21_ECOLX Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

See Also

3sfm, resolution 1.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3sfm&oldid=4097378"