1hrd: Difference between revisions

Revision as of 14:04, 21 February 2008

GLUTAMATE DEHYDROGENASE

OverviewOverview

BACKGROUND: The hyperthermophile Pyrococcus furiosus is one of the most thermostable organisms known, with an optimum growth temperature of 100 degrees C. The proteins from this organism display extreme thermostability. We have undertaken the structure determination of glutamate dehydrogenase from P. furiosus in order to gain further insights into the relationship between molecular structure and thermal stability. RESULTS: The structure of P. furiosus glutamate dehydrogenase, a homohexameric enzyme, has been determined at 2.2 A resolution and compared with the structure of glutamate dehydrogenase from the mesophile Clostridium symbiosum. CONCLUSIONS: Comparison of the structures of these two enzymes has revealed one major difference: the structure of the hyperthermophilic enzyme contains a striking series of ion-pair networks on the surface of the protein subunits and buried at both interdomain and intersubunit interfaces. We propose that the formation of such extended networks may represent a major stabilizing feature associated with the adaptation of enzymes to extreme temperatures.

About this StructureAbout this Structure

1HRD is a Single protein structure of sequence from Clostridium symbiosum. Active as Glutamate dehydrogenase, with EC number 1.4.1.2 Full crystallographic information is available from OCA.

ReferenceReference

The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures., Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V, Structure. 1995 Nov 15;3(11):1147-58. PMID:8591026

Page seeded by OCA on Thu Feb 21 13:04:04 2008

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OCA

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-[[Image:1hrd.gif|left|200px]]<br /><applet load="1hrd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hrd.gif|left|200px]]<br /><applet load="1hrd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hrd, resolution 1.96&Aring;" />
 '''GLUTAMATE DEHYDROGENASE'''<br />
 ==Overview==
-BACKGROUND: The hyperthermophile Pyrococcus furiosus is one of the most, thermostable organisms known, with an optimum growth temperature of 100, degrees C. The proteins from this organism display extreme, thermostability. We have undertaken the structure determination of, glutamate dehydrogenase from P. furiosus in order to gain further insights, into the relationship between molecular structure and thermal stability., RESULTS: The structure of P. furiosus glutamate dehydrogenase, a, homohexameric enzyme, has been determined at 2.2 A resolution and compared, with the structure of glutamate dehydrogenase from the mesophile, Clostridium symbiosum. CONCLUSIONS: Comparison of the structures of these, two enzymes has revealed one major difference: the structure of the, hyperthermophilic enzyme contains a striking series of ion-pair networks, on the surface of the protein subunits and buried at both interdomain and, intersubunit interfaces. We propose that the formation of such extended, networks may represent a major stabilizing feature associated with the, adaptation of enzymes to extreme temperatures.
+BACKGROUND: The hyperthermophile Pyrococcus furiosus is one of the most thermostable organisms known, with an optimum growth temperature of 100 degrees C. The proteins from this organism display extreme thermostability. We have undertaken the structure determination of glutamate dehydrogenase from P. furiosus in order to gain further insights into the relationship between molecular structure and thermal stability. RESULTS: The structure of P. furiosus glutamate dehydrogenase, a homohexameric enzyme, has been determined at 2.2 A resolution and compared with the structure of glutamate dehydrogenase from the mesophile Clostridium symbiosum. CONCLUSIONS: Comparison of the structures of these two enzymes has revealed one major difference: the structure of the hyperthermophilic enzyme contains a striking series of ion-pair networks on the surface of the protein subunits and buried at both interdomain and intersubunit interfaces. We propose that the formation of such extended networks may represent a major stabilizing feature associated with the adaptation of enzymes to extreme temperatures.
 ==About this Structure==
-HRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Active as [http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HRD OCA].
+HRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Active as [http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRD OCA].
 ==Reference==
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 [[Category: Glutamate dehydrogenase]]
 [[Category: Single protein]]
-[[Category: Baker, P.J.]]
+[[Category: Baker, P J.]]
-[[Category: Britton, K.L.]]
+[[Category: Britton, K L.]]
-[[Category: Rice, D.W.]]
+[[Category: Rice, D W.]]
-[[Category: Stillman, T.J.]]
+[[Category: Stillman, T J.]]
 [[Category: nad]]
 [[Category: oxidoreductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:46:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:04 2008''