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2bwh

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Revision as of 07:01, 12 December 2018

Laue Structure of a Short Lived State of L29W Myoglobin

Structural highlights

2bwh is a 1 chain structure with sequence from Phycd. 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, 1f6h, 1fcs, 1h1x, 1hjt, 1iop, 1irc, 1j3f, 1j52, 1jdo, 1jp6, 1jp8, 1jp9, 1jpb, 1jw8, 1l2k, 1ltw, 1lue, 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, 1myz, 1mz0, 1n9f, 1n9h, 1n9i, 1n9x, 1naz, 1o16, 1obm, 1ofj, 1ofk, 1spe, 1swm, 1tes, 1ufj, 1ufp, 1vxa, 1vxb, 1vxc, 1vxd, 1vxe, 1vxf, 1vxg, 1vxh, 1wvp, 1yog, 1yoh, 1yoi, 2blh, 2bli, 2blj, 2bw9, 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
Gene:	MB (PHYCD)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYG_PHYCD] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

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

By using time-resolved x-ray crystallography at room temperature, structural relaxations and ligand migration were examined in myoglobin (Mb) mutant L29W from nanoseconds to seconds after photodissociation of carbon monoxide (CO) from the heme iron by nanosecond laser pulses. The data were analyzed in terms of transient kinetics by fitting trial functions to integrated difference electron density values obtained from select structural moieties, thus allowing a quantitative description of the processes involved. The observed relaxations are linked to other investigations on protein dynamics. At the earliest times, the heme has already completely relaxed into its domed deoxy structure, and there is no photo-dissociated CO visible at the primary docking site. Initial relaxations of larger globin moieties are completed within several hundred nanoseconds. They influence the concomitant migration of photo-dissociated CO to the Xe1 site, where it appears at approximately 300 ns and leaves again at approximately 1.5 ms. The extremely long residence time in Xe1 as compared with wild-type MbCO implies that, in the latter protein, the CO exits the protein from Xe1 predominantly via the distal pocket. A well-defined deligated state is populated between approximately 2 micros and approximately 1 ms; its structure is very similar to the equilibrium deoxy structure. Between 1.5 and 20 ms, no CO is visible in the protein interior; it is either distributed among many sites within the protein or has escaped to the solvent. Finally, recombination at the heme iron occurs after >20 ms.

Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO.,Schmidt M, Nienhaus K, Pahl R, Krasselt A, Anderson S, Parak F, Nienhaus GU, Srajer V Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11704-9. Epub 2005 Aug 5. PMID:16085709^[1]

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

References

↑ Schmidt M, Nienhaus K, Pahl R, Krasselt A, Anderson S, Parak F, Nienhaus GU, Srajer V. Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO. Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11704-9. Epub 2005 Aug 5. PMID:16085709

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bwh"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bwh' size='340' side='right' caption='[[2bwh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bwh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BWH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bwh]] 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=2BWH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BWH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]], [[1f6h|1f6h]], [[1fcs|1fcs]], [[1h1x|1h1x]], [[1hjt|1hjt]], [[1iop|1iop]], [[1irc|1irc]], [[1j3f|1j3f]], [[1j52|1j52]], [[1jdo|1jdo]], [[1jp6|1jp6]], [[1jp8|1jp8]], [[1jp9|1jp9]], [[1jpb|1jpb]], [[1jw8|1jw8]], [[1l2k|1l2k]], [[1ltw|1ltw]], [[1lue|1lue]], [[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]], [[1myz|1myz]], [[1mz0|1mz0]], [[1n9f|1n9f]], [[1n9h|1n9h]], [[1n9i|1n9i]], [[1n9x|1n9x]], [[1naz|1naz]], [[1o16|1o16]], [[1obm|1obm]], [[1ofj|1ofj]], [[1ofk|1ofk]], [[1spe|1spe]], [[1swm|1swm]], [[1tes|1tes]], [[1ufj|1ufj]], [[1ufp|1ufp]], [[1vxa|1vxa]], [[1vxb|1vxb]], [[1vxc|1vxc]], [[1vxd|1vxd]], [[1vxe|1vxe]], [[1vxf|1vxf]], [[1vxg|1vxg]], [[1vxh|1vxh]], [[1wvp|1wvp]], [[1yog|1yog]], [[1yoh|1yoh]], [[1yoi|1yoi]], [[2blh|2blh]], [[2bli|2bli]], [[2blj|2blj]], [[2bw9|2bw9]], [[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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYCD])</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=2bwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bwh OCA], [http://pdbe.org/2bwh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bwh RCSB], [http://www.ebi.ac.uk/pdbsum/2bwh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bwh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/2bwh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/2bwh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
+[[Category: Phycd]]
 [[Category: Anderson, S]]
 [[Category: Krasselt, A]]

2bwh

From Proteopedia

Revision as of 07:01, 12 December 2018

Laue Structure of a Short Lived State of L29W Myoglobin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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