1ebg: Difference between revisions

Line 1:

[[Image:1ebg.gif|left|200px]]<br /><applet load="1ebg" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ebg.gif|left|200px]]<br /><applet load="1ebg" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ebg, resolution 2.1Å" />

'''CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION'''<br />

==Overview==

The structure of a new crystal form of enolase from bakers' yeast has been, solved to 2.1-A resolution. Crystals were grown from poly(ethylene glycol), and KCl at pH 8.2 in the presence of Mg2+ and a reaction intermediate, analog, phosphonoacetohydroxamate (PhAH). Crystals belong to space group, C2; have unit cell dimensions a = 123.5 A, b = 73.9 A, and c = 94.8 A with, beta = 93.3 degrees; and contain one dimer per asymmetric unit. The, structure was solved by molecular replacement from the X-ray coordinates, of apoenolase [Stec, B., & Lebioda, L. (1990) J. Mol. Biol. 211, 235-248]., Both essential divalent metal ions are observed to be complexed with the, inhibitor. The two Mg2+ ions are 4.05 A apart and are bridged by a mu-oxyl, ligand from the carbonyl moiety of PhAH. The "high-affinity" Mg2+, coordinates to the carboxylate side chains of Asp 246, Glu 295, and Asp, 320, one water molecule, and the hydroxamate and carbonyl oxygens of PhAH., The second Mg2+ coordinates to a phosphonyl oxygen, two water molecules, and the mu-bridge carbonyl oxygen of PhAH. Coordination schemes with, respect to PhAH and water ligands are fully consistent with those of the, Mn2+ complexes determined spectroscopically [Poyner, R.R., & Reed, G. H., (1992) Biochemistry 31, 7166-7173]. Remaining ligands for the second Mg2+, are the carbonyl oxygen and gamma-oxygen of Ser 39. Chelation of this Ser, residue to Mg2+ effectively "latches" a flexible loop extending from Gly, 37 through His 43 and closes off the entrance to the active site. The, position of the second Mg2+ in the active site provides new insight into, the stereochemistry of substrate binding.

The structure of a new crystal form of enolase from bakers' yeast has been solved to 2.1-A resolution. Crystals were grown from poly(ethylene glycol) and KCl at pH 8.2 in the presence of Mg2+ and a reaction intermediate analog, phosphonoacetohydroxamate (PhAH). Crystals belong to space group C2; have unit cell dimensions a = 123.5 A, b = 73.9 A, and c = 94.8 A with beta = 93.3 degrees; and contain one dimer per asymmetric unit. The structure was solved by molecular replacement from the X-ray coordinates of apoenolase [Stec, B., & Lebioda, L. (1990) J. Mol. Biol. 211, 235-248]. Both essential divalent metal ions are observed to be complexed with the inhibitor. The two Mg2+ ions are 4.05 A apart and are bridged by a mu-oxyl ligand from the carbonyl moiety of PhAH. The "high-affinity" Mg2+ coordinates to the carboxylate side chains of Asp 246, Glu 295, and Asp 320, one water molecule, and the hydroxamate and carbonyl oxygens of PhAH. The second Mg2+ coordinates to a phosphonyl oxygen, two water molecules, and the mu-bridge carbonyl oxygen of PhAH. Coordination schemes with respect to PhAH and water ligands are fully consistent with those of the Mn2+ complexes determined spectroscopically [Poyner, R.R., & Reed, G. H. (1992) Biochemistry 31, 7166-7173]. Remaining ligands for the second Mg2+ are the carbonyl oxygen and gamma-oxygen of Ser 39. Chelation of this Ser residue to Mg2+ effectively "latches" a flexible loop extending from Gly 37 through His 43 and closes off the entrance to the active site. The position of the second Mg2+ in the active site provides new insight into the stereochemistry of substrate binding.

==About this Structure==

1EBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and PAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1EBG OCA].

1EBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PAH:'>PAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBG OCA].

==Reference==

Line 15:

[[Category: Single protein]]

[[Category: Rayment, I.]]

[[Category: Reed, G.H.]]

[[Category: Reed, G H.]]

[[Category: Wedekind, J.E.]]

[[Category: Wedekind, J E.]]

[[Category: MG]]

[[Category: PAH]]

[[Category: carbon-oxygen lyase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:02 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ebg.gif|left|200px]]<br /><applet load="1ebg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ebg.gif|left|200px]]<br /><applet load="1ebg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ebg, resolution 2.1&Aring;" />
 '''CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The structure of a new crystal form of enolase from bakers' yeast has been, solved to 2.1-A resolution. Crystals were grown from poly(ethylene glycol), and KCl at pH 8.2 in the presence of Mg2+ and a reaction intermediate, analog, phosphonoacetohydroxamate (PhAH). Crystals belong to space group, C2; have unit cell dimensions a = 123.5 A, b = 73.9 A, and c = 94.8 A with, beta = 93.3 degrees; and contain one dimer per asymmetric unit. The, structure was solved by molecular replacement from the X-ray coordinates, of apoenolase [Stec, B., &amp; Lebioda, L. (1990) J. Mol. Biol. 211, 235-248]., Both essential divalent metal ions are observed to be complexed with the, inhibitor. The two Mg2+ ions are 4.05 A apart and are bridged by a mu-oxyl, ligand from the carbonyl moiety of PhAH. The "high-affinity" Mg2+, coordinates to the carboxylate side chains of Asp 246, Glu 295, and Asp, 320, one water molecule, and the hydroxamate and carbonyl oxygens of PhAH., The second Mg2+ coordinates to a phosphonyl oxygen, two water molecules, and the mu-bridge carbonyl oxygen of PhAH. Coordination schemes with, respect to PhAH and water ligands are fully consistent with those of the, Mn2+ complexes determined spectroscopically [Poyner, R.R., &amp; Reed, G. H., (1992) Biochemistry 31, 7166-7173]. Remaining ligands for the second Mg2+, are the carbonyl oxygen and gamma-oxygen of Ser 39. Chelation of this Ser, residue to Mg2+ effectively "latches" a flexible loop extending from Gly, 37 through His 43 and closes off the entrance to the active site. The, position of the second Mg2+ in the active site provides new insight into, the stereochemistry of substrate binding.
+The structure of a new crystal form of enolase from bakers' yeast has been solved to 2.1-A resolution. Crystals were grown from poly(ethylene glycol) and KCl at pH 8.2 in the presence of Mg2+ and a reaction intermediate analog, phosphonoacetohydroxamate (PhAH). Crystals belong to space group C2; have unit cell dimensions a = 123.5 A, b = 73.9 A, and c = 94.8 A with beta = 93.3 degrees; and contain one dimer per asymmetric unit. The structure was solved by molecular replacement from the X-ray coordinates of apoenolase [Stec, B., &amp; Lebioda, L. (1990) J. Mol. Biol. 211, 235-248]. Both essential divalent metal ions are observed to be complexed with the inhibitor. The two Mg2+ ions are 4.05 A apart and are bridged by a mu-oxyl ligand from the carbonyl moiety of PhAH. The "high-affinity" Mg2+ coordinates to the carboxylate side chains of Asp 246, Glu 295, and Asp 320, one water molecule, and the hydroxamate and carbonyl oxygens of PhAH. The second Mg2+ coordinates to a phosphonyl oxygen, two water molecules, and the mu-bridge carbonyl oxygen of PhAH. Coordination schemes with respect to PhAH and water ligands are fully consistent with those of the Mn2+ complexes determined spectroscopically [Poyner, R.R., &amp; Reed, G. H. (1992) Biochemistry 31, 7166-7173]. Remaining ligands for the second Mg2+ are the carbonyl oxygen and gamma-oxygen of Ser 39. Chelation of this Ser residue to Mg2+ effectively "latches" a flexible loop extending from Gly 37 through His 43 and closes off the entrance to the active site. The position of the second Mg2+ in the active site provides new insight into the stereochemistry of substrate binding.
 ==About this Structure==
-EBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and PAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EBG OCA].
+EBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PAH:'>PAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBG OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Rayment, I.]]
-[[Category: Reed, G.H.]]
+[[Category: Reed, G H.]]
-[[Category: Wedekind, J.E.]]
+[[Category: Wedekind, J E.]]
 [[Category: MG]]
 [[Category: PAH]]
 [[Category: carbon-oxygen lyase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:52:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:02 2008''