1ghg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1ghg" [edit=sysop:move=sysop])
Current revision (23:31, 27 December 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ghg.png|left|200px]]
 
-
<!--
+
==CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON==
-
The line below this paragraph, containing "STRUCTURE_1ghg", creates the "Structure Box" on the page.
+
<StructureSection load='1ghg' size='340' side='right'caption='[[1ghg]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1ghg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHG FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.98&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3FG:(2S)-AMINO(3,5-DIHYDROXYPHENYL)ETHANOIC+ACID'>3FG</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</scene>, <scene name='pdbligand=OMY:(BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE'>OMY</scene>, <scene name='pdbligand=OMZ:(BETAR)-3-CHLORO-BETA-HYDROXY-D-TYROSINE'>OMZ</scene>, <scene name='pdbligand=PRD_000206:VANCOMYCIN+AGLYCON'>PRD_000206</scene></td></tr>
-
{{STRUCTURE_1ghg| PDB=1ghg | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ghg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghg OCA], [https://pdbe.org/1ghg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghg RCSB], [https://www.ebi.ac.uk/pdbsum/1ghg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghg ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The sugar residues of the glycopeptide antibiotic vancomycin contribute to the cooperativity of ligand binding, thereby increasing ligand affinity and enhancing antimicrobial activity. To assess the structural basis for these effects, we determined a 0.98 A X-ray crystal structure of the vancomycin aglycon and compared it to structures of several intact vancomycin:ligand complexes. The crystal structure reveals that the aglycon binds acetate anions and forms back-to-back dimeric complexes in a manner similar to that of intact vancomycin. However, the four independent copies of the aglycon in each asymmetric unit of the crystal exhibit a high degree of conformational heterogeneity. These results suggest that the sugar residues, in addition to enlarging and strengthening the dimer interface, provide steric constraints that limit the vancomycin molecule to a relatively small number of productive conformations.
-
===CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON===
+
The role of sugar residues in molecular recognition by vancomycin.,Kaplan J, Korty BD, Axelsen PH, Loll PJ J Med Chem. 2001 May 24;44(11):1837-40. PMID:11356118<ref>PMID:11356118</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_11356118}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1ghg" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 11356118 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_11356118}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Amycolatopsis orientalis]]
-
[[1ghg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHG OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Axelsen PH]]
-
==Reference==
+
[[Category: Kaplan J]]
-
<ref group="xtra">PMID:011356118</ref><references group="xtra"/>
+
[[Category: Korty BD]]
-
[[Category: Axelsen, P H.]]
+
[[Category: Loll PJ]]
-
[[Category: Kaplan, J.]]
+
-
[[Category: Korty, B D.]]
+
-
[[Category: Loll, P J.]]
+
-
[[Category: Aglycon]]
+
-
[[Category: Antibiotic]]
+
-
[[Category: Glycopeptide]]
+
-
[[Category: Vancomycin]]
+

Current revision

CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON

PDB ID 1ghg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ghg"
Personal tools