1k9x

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(New page: 200px<br /><applet load="1k9x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k9x, resolution 2.30&Aring;" /> '''Structure of Pyrococ...)
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[[Image:1k9x.gif|left|200px]]<br /><applet load="1k9x" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1k9x.gif|left|200px]]<br /><applet load="1k9x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1k9x, resolution 2.30&Aring;" />
caption="1k9x, resolution 2.30&Aring;" />
'''Structure of Pyrococcus furiosus carboxypeptidase Apo-Yb'''<br />
'''Structure of Pyrococcus furiosus carboxypeptidase Apo-Yb'''<br />
==Overview==
==Overview==
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The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been, determined to 2.2 A resolution using multiwavelength anomalous diffraction, (MAD) methods. PfuCP represents the first structure of the new M32 family, of carboxypeptidases. The overall structure is comprised of a homodimer., Each subunit is mostly helical with its most pronounced feature being a, deep substrate binding groove. The active site lies at the bottom of this, groove and contains an HEXXH motif that coordinates the metal ion required, for catalysis. Surprisingly, the structure is similar to the recently, reported rat neurolysin. Comparison of these structures as well as, sequence analyses with other homologous proteins reveal several conserved, residues. The roles for these conserved residues in the catalytic, mechanism are inferred based on modeling and their location.
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The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.
==About this Structure==
==About this Structure==
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1K9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K9X OCA].
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1K9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9X OCA].
==Reference==
==Reference==
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[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arndt, J.W.]]
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[[Category: Arndt, J W.]]
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[[Category: Chan, M.K.]]
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[[Category: Chan, M K.]]
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[[Category: Chan, S.I.]]
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[[Category: Chan, S I.]]
[[Category: Cheng, T.]]
[[Category: Cheng, T.]]
[[Category: Hao, B.]]
[[Category: Hao, B.]]
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[[Category: metallopeptidase]]
[[Category: metallopeptidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:00:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:45 2008''

Revision as of 11:31, 21 February 2008


1k9x, resolution 2.30Å

Drag the structure with the mouse to rotate

Structure of Pyrococcus furiosus carboxypeptidase Apo-Yb

Overview

The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.

About this Structure

1K9X is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus., Arndt JW, Hao B, Ramakrishnan V, Cheng T, Chan SI, Chan MK, Structure. 2002 Feb;10(2):215-24. PMID:11839307

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