1ash

From Proteopedia

(Difference between revisions)

Revision as of 08:08, 11 September 2015

THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY

Structural highlights

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

Function

[GLB_ASCSU] Has an extremely high oxygen affinity. In a vacuum, it takes several minutes to release its oxygen compared to milliseconds for a normal globin. Could be used as an oxygen scavenger for sterol biosynthesis.

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 perienteric hemoglobin of the parasitic nematode Ascaris has an exceptionally high affinity for oxygen. It is an octameric protein containing two similar heme-binding domains per subunit, but recombinant constructs expressing a single, monomeric heme-binding domain (domain 1; D1) retain full oxygen avidity. We have solved the crystal structure of D1 at 2.2 A resolution. Analysis of the structure reveals a characteristic globin fold and illuminates molecular features involved in oxygen avidity of Ascaris perienteric hemoglobin. A strong hydrogen bond between tyrosine at position 10 in the B helix (tyrosine-B10) and the distal oxygen of the ligand, combined with a weak hydrogen bond between glutamine-E7 and the proximal oxygen, grips the ligand in the binding pocket. A third hydrogen bond between these two amino acids appears to stabilize the structure. The B helix of D1 is displaced laterally by 2.5 A when compared with sperm whale myoglobin. This shifts the tyrosine-B10 hydroxyl far enough from liganded oxygen to form a strong hydrogen bond without steric hindrance. Changes in the F helix compared with myoglobin contribute to a tilted heme that may also be important for oxygen affinity.

The structure of Ascaris hemoglobin domain I at 2.2 A resolution: molecular features of oxygen avidity.,Yang J, Kloek AP, Goldberg DE, Mathews FS Proc Natl Acad Sci U S A. 1995 May 9;92(10):4224-8. PMID:7753786^[1]

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

References

↑ Yang J, Kloek AP, Goldberg DE, Mathews FS. The structure of Ascaris hemoglobin domain I at 2.2 A resolution: molecular features of oxygen avidity. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4224-8. PMID:7753786

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/1ash"

@@ Line 2: / Line 2: @@
 <StructureSection load='1ash' size='340' side='right' caption='[[1ash]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ash]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ASH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ash]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascsu Ascsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ASH 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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ash OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ash RCSB], [http://www.ebi.ac.uk/pdbsum/1ash 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=1ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ash OCA], [http://pdbe.org/1ash PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ash RCSB], [http://www.ebi.ac.uk/pdbsum/1ash PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ash" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Ascaris suum]]
+[[Category: Ascsu]]
 [[Category: Goldberg, D E]]
 [[Category: Kloek, A P]]

1ash

From Proteopedia

Revision as of 08:08, 11 September 2015

THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN I AT 2.2 ANGSTROMS RESOLUTION: MOLECULAR FEATURES OF OXYGEN AVIDITY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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