2h4l: Difference between revisions

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New page: left|200px<br /><applet load="2h4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h4l, resolution 2.40Å" /> '''Complex of PMM/PGM w...
 
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[[Image:2h4l.gif|left|200px]]<br /><applet load="2h4l" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2h4l.gif|left|200px]]<br /><applet load="2h4l" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2h4l, resolution 2.40&Aring;" />
caption="2h4l, resolution 2.40&Aring;" />
'''Complex of PMM/PGM with ribose 1-phosphate'''<br />
'''Complex of PMM/PGM with ribose 1-phosphate'''<br />


==Overview==
==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.
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==
2H4L 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 R1P and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H4L OCA].  
2H4L 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=R1P:'>R1P</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H4L OCA].  


==Reference==
==Reference==
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]
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]]
[[Category: Beamer, L.J.]]
[[Category: Beamer, L J.]]
[[Category: R1P]]
[[Category: R1P]]
[[Category: ZN]]
[[Category: ZN]]
Line 20: Line 20:
[[Category: slow substrate]]
[[Category: slow substrate]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:32:33 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:38:08 2008''

Revision as of 18:38, 21 February 2008

File:2h4l.gif


2h4l, resolution 2.40Å

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Complex of PMM/PGM with ribose 1-phosphate

OverviewOverview

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 StructureAbout this Structure

2H4L is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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 17:38:08 2008

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