1v07

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[[Image:1v07.gif|left|200px]]<br /><applet load="1v07" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v07.gif|left|200px]]
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caption="1v07, resolution 1.70&Aring;" />
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'''CRYSTAL STRUCTURE OF THRE11VAL MUTANT OF THE NERVE TISSUE MINI-HEMOGLOBIN FROM THE NEMERTEAN WORM CEREBRATULUS LACTEUS'''<br />
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{{Structure
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|PDB= 1v07 |SIZE=350|CAPTION= <scene name='initialview01'>1v07</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=AC1:So4+Environment+In+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=OXY:OXYGEN MOLECULE'>OXY</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THRE11VAL MUTANT OF THE NERVE TISSUE MINI-HEMOGLOBIN FROM THE NEMERTEAN WORM CEREBRATULUS LACTEUS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1V07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Environment+In+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V07 OCA].
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1V07 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V07 OCA].
==Reference==
==Reference==
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Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin., Pesce A, Nardini M, Ascenzi P, Geuens E, Dewilde S, Moens L, Bolognesi M, Riggs AF, Hale A, Deng P, Nienhaus GU, Olson JS, Nienhaus K, J Biol Chem. 2004 Aug 6;279(32):33662-72. Epub 2004 May 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15161908 15161908]
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Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin., Pesce A, Nardini M, Ascenzi P, Geuens E, Dewilde S, Moens L, Bolognesi M, Riggs AF, Hale A, Deng P, Nienhaus GU, Olson JS, Nienhaus K, J Biol Chem. 2004 Aug 6;279(32):33662-72. Epub 2004 May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15161908 15161908]
[[Category: Cerebratulus lacteus]]
[[Category: Cerebratulus lacteus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxygen affinity of c lacteus mini-hemoglobin]]
[[Category: oxygen affinity of c lacteus mini-hemoglobin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:13 2008''

Revision as of 12:39, 20 March 2008

Image:1v07.gif


PDB ID 1v07

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THRE11VAL MUTANT OF THE NERVE TISSUE MINI-HEMOGLOBIN FROM THE NEMERTEAN WORM CEREBRATULUS LACTEUS


Overview

The mini-hemoglobin from Cerebratulus lacteus (CerHb) belongs to a class of globins containing the polar Tyr-B10/Gln-E7 amino acid pair that normally causes low rates of O2 dissociation and ultra-high O2 affinity, which suggest O2 sensing or NO scavenging functions. CerHb, however, has high rates of O2 dissociation (kO2 = 200-600 s(-1)) and moderate O2 affinity (KO2) approximately 1 microm(-1)) as a result of a third polar amino acid in its active site, Thr-E11. When Thr-E11 is replaced by Val, kO2 decreases 1000-fold and KO2 increases 130-fold at pH 7.0, 20 degrees C. The mutation also shifts the stretching frequencies of both heme-bound and photodissociated CO, indicating marked changes of the electrostatic field at the active site. The crystal structure of Thr-E11 --> Val CerHbO2 at 1.70 A resolution is almost identical to that of the wild-type protein (root mean square deviation of 0.12 A). The dramatic functional and spectral effects of the Thr-E11 --> Val mutation are due exclusively to changes in the hydrogen bonding network in the active site. Replacing Thr-E11 with Val "frees" the Tyr-B10 hydroxyl group to rotate toward and donate a strong hydrogen bond to the heme-bound ligand, causing a selective increase in O2 affinity, a decrease of the rate coefficient for O2 dissociation, a 40 cm(-1) decrease in nuCO of heme-bound CO, and an increase in ligand migration toward more remote intermediate sites.

About this Structure

1V07 is a Single protein structure of sequence from Cerebratulus lacteus. Full crystallographic information is available from OCA.

Reference

Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin., Pesce A, Nardini M, Ascenzi P, Geuens E, Dewilde S, Moens L, Bolognesi M, Riggs AF, Hale A, Deng P, Nienhaus GU, Olson JS, Nienhaus K, J Biol Chem. 2004 Aug 6;279(32):33662-72. Epub 2004 May 25. PMID:15161908

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