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2h5a

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(New page: 200px<br /><applet load="2h5a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h5a, resolution 1.72&Aring;" /> '''Complex of the enzym...)
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[[Image:2h5a.gif|left|200px]]<br /><applet load="2h5a" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2h5a.gif|left|200px]]<br /><applet load="2h5a" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2h5a, resolution 1.72&Aring;" />
caption="2h5a, resolution 1.72&Aring;" />
'''Complex of the enzyme PMM/PGM with xylose 1-phosphate'''<br />
'''Complex of the enzyme PMM/PGM with xylose 1-phosphate'''<br />
==Overview==
==Overview==
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Two complexes of the enzyme phosphomannomutase/phosphoglucomutase, (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an, inhibitor have been characterized by X-ray crystallography. Both ligands, induce an interdomain rearrangement in the enzyme that creates a highly, buried active site. Comparisons with enzyme-substrate complexes show that, the inhibitor xylose 1-phosphate utilizes many of the previously observed, enzyme-ligand interactions. In contrast, analysis of the ribose, 1-phosphate complex reveals a combination of new and conserved, enzyme-ligand interactions for binding. The ability of PMM/PGM to, accommodate these two pentose phosphosugars in its active site may be, relevant for future efforts towards inhibitor design.
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Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.
==About this Structure==
==About this Structure==
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2H5A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN and X1P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H5A OCA].
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2H5A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=X1P:'>X1P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5A OCA].
==Reference==
==Reference==
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Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor., Regni C, Shackelford GS, Beamer LJ, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16880541 16880541]
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Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor., Regni C, Shackelford GS, Beamer LJ, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16880541 16880541]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beamer, L.J.]]
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[[Category: Beamer, L J.]]
[[Category: Regni, C.]]
[[Category: Regni, C.]]
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[[Category: Shackelford, G.S.]]
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[[Category: Shackelford, G S.]]
[[Category: X1P]]
[[Category: X1P]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: inhibitor]]
[[Category: inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:32:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:38:17 2008''

Revision as of 15:38, 21 February 2008


2h5a, resolution 1.72Å

Drag the structure with the mouse to rotate

Complex of the enzyme PMM/PGM with xylose 1-phosphate

Overview

Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.

About this Structure

2H5A is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.

Reference

Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor., Regni C, Shackelford GS, Beamer LJ, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:16880541

Page seeded by OCA on Thu Feb 21 17:38:17 2008

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