This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1h1x

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 04:45, 21 September 2017

Sperm whale Myoglobin mutant T67R S92D

Structural highlights

1h1x is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	101m, 102m, 103m, 104m, 105m, 106m, 107m, 108m, 109m, 110m, 111m, 112m, 1a6g, 1a6k, 1a6m, 1a6n, 1abs, 1ajg, 1ajh, 1bvc, 1bvd, 1bz6, 1bzp, 1bzr, 1ch1, 1ch2, 1ch3, 1ch5, 1ch7, 1ch9, 1cik, 1cio, 1co8, 1co9, 1cp0, 1cp5, 1cpw, 1cq2, 1do1, 1do3, 1do4, 1do7, 1dti, 1dtm, 1duk, 1duo, 1dxc, 1dxd, 1ebc, 1f63, 1f65, 1fcs, 1hjt, 1iop, 1irc, 1jdo, 1jp6, 1jp8, 1jp9, 1jpb, 1jw8, 1ltw, 1mbc, 1mbd, 1mbi, 1mbn, 1mbo, 1mcy, 1mgn, 1mlf, 1mlg, 1mlh, 1mlj, 1mlk, 1mll, 1mlm, 1mln, 1mlo, 1mlq, 1mlr, 1mls, 1mlu, 1moa, 1mob, 1moc, 1mod, 1mti, 1mtj, 1mtk, 1myf, 1mym, 1obm, 1ofj, 1ofk, 1spe, 1swm, 1tes, 1vxa, 1vxb, 1vxc, 1vxd, 1vxe, 1vxf, 1vxg, 1vxh, 1yog, 1yoh, 1yoi, 2cmm, 2mb5, 2mbw, 2mga, 2mgb, 2mgc, 2mgd, 2mge, 2mgf, 2mgg, 2mgh, 2mgi, 2mgj, 2mgk, 2mgl, 2mgm, 2mya, 2myb, 2myc, 2myd, 2mye, 2spl, 2spm, 2spn, 2spo, 4mbn, 5mbn
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Atomic co-ordinates and structure factors for the T67R/S92D metMbCN mutant have been deposited with the Protein Data Bank, under accession codes 1h1x and r1h1xsf, respectively. Protein engineering and cofactor replacement have been employed as tools to introduce/modulate peroxidase activity in sperm whale Mb (myoglobin). Based on the rationale that haem peroxidase active sites are characterized by specific charged residues, the Mb haem crevice has been modified to host a haem-distalpropionate Arg residue and a proximal Asp, yielding the T67R/S92D Mb mutant. To code extra conformational mobility around the haem, and to increase the peroxidase catalytic efficiency, the T67R/S92D Mb mutant has been subsequently reconstituted with protohaem-L-histidine methyl ester, yielding a stable derivative, T67R/S92D Mb-H. The crystal structure of T67R/S92D cyano-metMb (1.4 A resolution; R factor, 0.12) highlights a regular haem-cyanide binding mode, and the role for the mutated residues in affecting the haem propionates as well as the neighbouring water structure. The conformational disorder of the haem propionate-7 is evidenced by the NMR spectrum of the mutant. Ligand-binding studies show that the iron(III) centres of T67R/S92D Mb, and especially of T67R/S92D Mb-H, exhibit higher affinity for azide and imidazole than wild-type Mb. In addition, both protein derivatives react faster than wild-type Mb with hydrogen peroxide, showing higher peroxidase-like activity towards phenolic substrates. The catalytic efficiency of T67R/S92D Mb-H in these reactions is the highest so far reported for Mb derivatives. A model for the protein-substrate interaction is deduced based on the crystal structure and on the NMR spectra of protein-phenol complexes.

Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine.,Roncone R, Monzani E, Murtas M, Battaini G, Pennati A, Sanangelantoni AM, Zuccotti S, Bolognesi M, Casella L Biochem J. 2004 Feb 1;377(Pt 3):717-24. PMID:14563209^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Roncone R, Monzani E, Murtas M, Battaini G, Pennati A, Sanangelantoni AM, Zuccotti S, Bolognesi M, Casella L. Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine. Biochem J. 2004 Feb 1;377(Pt 3):717-24. PMID:14563209 doi:10.1042/BJ20030863

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h1x"

@@ Line 1: / Line 1: @@
-==SPERM WHALE MYOGLOBIN MUTANT T67R S92D==
+==Sperm whale Myoglobin mutant T67R S92D==
 <StructureSection load='1h1x' size='340' side='right' caption='[[1h1x]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h1x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H1X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h1x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H1X FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[101m|101m]], [[102m|102m]], [[103m|103m]], [[104m|104m]], [[105m|105m]], [[106m|106m]], [[107m|107m]], [[108m|108m]], [[109m|109m]], [[110m|110m]], [[111m|111m]], [[112m|112m]], [[1a6g|1a6g]], [[1a6k|1a6k]], [[1a6m|1a6m]], [[1a6n|1a6n]], [[1abs|1abs]], [[1ajg|1ajg]], [[1ajh|1ajh]], [[1bvc|1bvc]], [[1bvd|1bvd]], [[1bz6|1bz6]], [[1bzp|1bzp]], [[1bzr|1bzr]], [[1ch1|1ch1]], [[1ch2|1ch2]], [[1ch3|1ch3]], [[1ch5|1ch5]], [[1ch7|1ch7]], [[1ch9|1ch9]], [[1cik|1cik]], [[1cio|1cio]], [[1co8|1co8]], [[1co9|1co9]], [[1cp0|1cp0]], [[1cp5|1cp5]], [[1cpw|1cpw]], [[1cq2|1cq2]], [[1do1|1do1]], [[1do3|1do3]], [[1do4|1do4]], [[1do7|1do7]], [[1dti|1dti]], [[1dtm|1dtm]], [[1duk|1duk]], [[1duo|1duo]], [[1dxc|1dxc]], [[1dxd|1dxd]], [[1ebc|1ebc]], [[1f63|1f63]], [[1f65|1f65]], [[1fcs|1fcs]], [[1hjt|1hjt]], [[1iop|1iop]], [[1irc|1irc]], [[1jdo|1jdo]], [[1jp6|1jp6]], [[1jp8|1jp8]], [[1jp9|1jp9]], [[1jpb|1jpb]], [[1jw8|1jw8]], [[1ltw|1ltw]], [[1mbc|1mbc]], [[1mbd|1mbd]], [[1mbi|1mbi]], [[1mbn|1mbn]], [[1mbo|1mbo]], [[1mcy|1mcy]], [[1mgn|1mgn]], [[1mlf|1mlf]], [[1mlg|1mlg]], [[1mlh|1mlh]], [[1mlj|1mlj]], [[1mlk|1mlk]], [[1mll|1mll]], [[1mlm|1mlm]], [[1mln|1mln]], [[1mlo|1mlo]], [[1mlq|1mlq]], [[1mlr|1mlr]], [[1mls|1mls]], [[1mlu|1mlu]], [[1moa|1moa]], [[1mob|1mob]], [[1moc|1moc]], [[1mod|1mod]], [[1mti|1mti]], [[1mtj|1mtj]], [[1mtk|1mtk]], [[1myf|1myf]], [[1mym|1mym]], [[1obm|1obm]], [[1ofj|1ofj]], [[1ofk|1ofk]], [[1spe|1spe]], [[1swm|1swm]], [[1tes|1tes]], [[1vxa|1vxa]], [[1vxb|1vxb]], [[1vxc|1vxc]], [[1vxd|1vxd]], [[1vxe|1vxe]], [[1vxf|1vxf]], [[1vxg|1vxg]], [[1vxh|1vxh]], [[1yog|1yog]], [[1yoh|1yoh]], [[1yoi|1yoi]], [[2cmm|2cmm]], [[2mb5|2mb5]], [[2mbw|2mbw]], [[2mga|2mga]], [[2mgb|2mgb]], [[2mgc|2mgc]], [[2mgd|2mgd]], [[2mge|2mge]], [[2mgf|2mgf]], [[2mgg|2mgg]], [[2mgh|2mgh]], [[2mgi|2mgi]], [[2mgj|2mgj]], [[2mgk|2mgk]], [[2mgl|2mgl]], [[2mgm|2mgm]], [[2mya|2mya]], [[2myb|2myb]], [[2myc|2myc]], [[2myd|2myd]], [[2mye|2mye]], [[2spl|2spl]], [[2spm|2spm]], [[2spn|2spn]], [[2spo|2spo]], [[4mbn|4mbn]], [[5mbn|5mbn]]</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=1h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1x OCA], [http://pdbe.org/1h1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h1x RCSB], [http://www.ebi.ac.uk/pdbsum/1h1x PDBsum]</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=1h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1x OCA], [http://pdbe.org/1h1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h1x RCSB], [http://www.ebi.ac.uk/pdbsum/1h1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h1x ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 15: / Line 16: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h1x ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Phycd]]
 [[Category: Bolognesi, M]]
 [[Category: Zuccotti, S]]

1h1x

From Proteopedia

Revision as of 04:45, 21 September 2017

Sperm whale Myoglobin mutant T67R S92D

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox