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.

1lhs

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:45, 18 August 2021

LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)

Structural highlights

1lhs is a 1 chain structure with sequence from Carcr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYG_CARCR] 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

The X-ray crystal structures of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin have been determined at 2.0 A resolution (R = 0.182, and 0.178, respectively). The results here reported, representing the first reptile globin solved by X-ray crystallography, have been analyzed in parallel with data for related monomeric hemoproteins, and indicate a strong overall structural similarity between the loggerhead sea turtle and mammalian myoglobins, reflected by the 63% amino acid identity of their primary structures. The root-mean-square deviation between the entire polypeptide backbones of loggerhead sea turtle and sperm whale myoglobins, after structure superposition, is 0.83 A. Upon cyanide binding to the protein distal site, the iron-bound water molecule present in the aquo-met form is displaced by the incoming ligand. Cyanide is oriented towards the inner part of the heme distal site forming a Fe-C-N angle of 133 degrees.

Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution.,Nardini M, Tarricone C, Rizzi M, Lania A, Desideri A, De Sanctis G, Coletta M, Petruzzelli R, Ascenzi P, Coda A, et al. J Mol Biol. 1995 Mar 31;247(3):459-65. PMID:7714901^[1]

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

References

↑ Nardini M, Tarricone C, Rizzi M, Lania A, Desideri A, De Sanctis G, Coletta M, Petruzzelli R, Ascenzi P, Coda A, et al.. Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution. J Mol Biol. 1995 Mar 31;247(3):459-65. PMID:7714901

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/1lhs"

@@ Line 3: / Line 3: @@
 <StructureSection load='1lhs' size='340' side='right'caption='[[1lhs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lhs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Carcr Carcr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LHS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lhs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carcr Carcr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LHS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1lhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lhs OCA], [http://pdbe.org/1lhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lhs RCSB], [http://www.ebi.ac.uk/pdbsum/1lhs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lhs ProSAT]</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=1lhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lhs OCA], [https://pdbe.org/1lhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lhs RCSB], [https://www.ebi.ac.uk/pdbsum/1lhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lhs ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYG_CARCR MYG_CARCR]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[[https://www.uniprot.org/uniprot/MYG_CARCR MYG_CARCR]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1lhs

From Proteopedia

Revision as of 06:45, 18 August 2021

LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox